Journal articles: 'Histidine peptide'

1

Gill, J. S., Y. Yiangou, D. J. Webb, L. Meleagros, N. Benjamin, B. J. Chrysanthou, J. R. Cockcroft, R. C. Causon, A. J. Camm, and S. R. Bloom. "Peptide histidine valine: Its haemodynamic actions and pharmacokinetics in man differ from those of vasoactive intestinal peptide and peptide histidine methionine." Clinical Science 78, no. 5 (May 1, 1990): 487–92. http://dx.doi.org/10.1042/cs0780487.

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1. The effects of intravenous and intra-arterial infusion of the peptides derived from prepro-vasoactive intestinal peptide, vasoactive intestinal peptide, peptide histidine methionine and peptide histidine valine, were examined in six healthy volunteers. 2. Vasoactive intestinal peptide given intravenously caused a significant increase in heart rate and a decrease in diastolic, but not systolic, blood presure, whereas peptide histidine valine caused an increase in heart rate alone, despite higher achieved circulating peptide concentrations. Peptide histidine methionine did not affect heart rate or blood pressure. Forearm blood flow was increased by vasoactive intestinal peptide and peptide histidine valine when infused locally intra-arterially, although vasoactive intestinal peptide was more potent than peptide histidine valine. 3. Plasma concentrations of cardiodilatin (the N-terminal peptide derived from pro-atrial natriuretic peptide) were increased by intravenous infusion of vasoactive intestinal peptide, but were unaffected by peptide histidine methionine or peptide histidine valine. Circulating plasma concentrations of adrenaline and noradrenaline did not change during infusion of vasoactive intestinal peptide, peptide histidine methionine or peptide histidine valine. 4. Peptide histidine valine had a long half-life when compared with peptide histidine methionine and vasoactive intestinal peptide. 5. We conclude that peptide histidine valine is active in the human cardiovascular system and has a similar, though less potent, vasodilating action to vasoactive intestinal peptide. The higher circulating levels of peptide histidine valine found in man suggest that it may be important in modulating vascular tone.

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Backwell, F. R. C., B. J. Bequette, L. A. Crompton, C. K. Reynolds, D. E. Beever, and J. C. MacRae. "Effect of intravenous histidine or histidine peptide infusion on milk protein yield in lactating goats with an induced histidine deficiency." Proceedings of the British Society of Animal Science 1996 (March 1996): 180. http://dx.doi.org/10.1017/s1752756200593752.

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Studies involving infusion of stable isotope labelled peptides have shown that the mammary gland has the ability to utilise peptide-derived AA for milk protein synthesis (Backwell et al., 1994a) and that peptides may be involved in the supply of phenylalanine to the mammary gland in vivo (Backwell et al., 1994b). The aim of the present experiment was to compare milk production responses to systemic (jugular vein) provision of histidine as free AA or as a peptide (glycyl-histidine) in lactating dairy goats with an induced histidine deficiency.

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Backwell, F. R. C., B. J. Bequette, L. A. Crompton, C. K. Reynolds, D. E. Beever, and J. C. MacRae. "Effect of intravenous histidine or histidine peptide infusion on milk protein yield in lactating goats with an induced histidine deficiency." Proceedings of the British Society of Animal Science 1996 (March 1996): 180. http://dx.doi.org/10.1017/s0308229600031469.

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Studies involving infusion of stable isotope labelled peptides have shown that the mammary gland has the ability to utilise peptide-derived AA for milk protein synthesis (Backwell et al., 1994a) and that peptides may be involved in the supply of phenylalanine to the mammary gland in vivo (Backwell et al., 1994b). The aim of the present experiment was to compare milk production responses to systemic (jugular vein) provision of histidine as free AA or as a peptide (glycyl-histidine) in lactating dairy goats with an induced histidine deficiency.

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Rigel, D. F. "Effects of neuropeptides on heart rate in dogs: comparison of VIP, PHI, NPY, CGRP, and NT." American Journal of Physiology-Heart and Circulatory Physiology 255, no. 2 (August 1, 1988): H311—H317. http://dx.doi.org/10.1152/ajpheart.1988.255.2.h311.

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This study was designed to evaluate the potential chronotropic actions of several cardiac neuropeptides in pentobarbital-anesthetized dogs. After bilateral vagotomy and stellectomy and muscarinic receptor blockade, I injected vasoactive intestinal polypeptide, peptide histidine isoleucine, neuropeptide Y, neurotensin, and calcitonin gene-related peptide into the intact sinus node artery. Neurotensin, calcitonin gene-related peptide, and neuropeptide Y exhibited no physiologically significant changes in heart rate. However, the structural homologues vasoactive intestinal polypeptide and peptide histidine isoleucine each augmented heart rate with maximal increases (approximately 120 beats/min) similar to those of norepinephrine. Vasoactive intestinal polypeptide and peptide histidine isoleucine were twice and 1/18, respectively, as potent as norepinephrine. The cardioacceleratory responses to vasoactive intestinal polypeptide and peptide histidine isoleucine were more slowly developing and longer lasting than those of norepinephrine. The responses to these two peptides were unchanged after beta-adrenergic blockade with propranolol in a dose sufficient to eliminate or greatly attenuate the norepinephrine tachycardia. These results indicate a potential role of endogenous vasoactive intestinal polypeptide and peptide histidine isoleucine in nonadrenergic, noncholinergic heart rate control in the dog.

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VANGURI, Vijay K., Shuxia WANG, Svetlana GODYNA, Sripriya RANGANATHAN, and Gene LIAU. "Thrombospondin-1 binds to polyhistidine with high affinity and specificity." Biochemical Journal 347, no. 2 (April 10, 2000): 469–73. http://dx.doi.org/10.1042/bj3470469.

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Thrombospondin-1 (TSP1) is a secreted trimeric glycoprotein of 450 kDa with demonstrated effects on cell growth, adhesion and migration. Its complex biological activity is attributed to its ability to bind to cell-surface receptors, growth factors and extracellular-matrix proteins. In this study, we used a 125I solid-phase binding assay to demonstrate that TSP1 binds specifically to proteins containing polyhistidine stretches. Based on studies with three different six-histidine-containing recombinant proteins, we derived an average dissociation constant of 5 nM. The binding of 125I-labelled TSP1 to these proteins was inhibited by peptides containing histidine residues, with the degree of competition being a function of the number of histidines within the peptide. Binding was not inhibited by excess histidine or imidazole, indicating that the imidazole ring is not sufficient for recognition by TSP1. Heparin was a potent inhibitor of binding with a Ki of 50 nM, suggesting that the heparin-binding domain of TSP1 may be involved in this interaction. This was confirmed by the ability of a recombinant heparin-binding domain of TSP1 to directly compete for TSP1 binding to polyhistidine-containing proteins. Affinity chromatography with a polyhistidine-containing peptide immobilized on agarose revealed that TSP1 in platelet releasates is the major polypeptide retained on the six-histidine-peptide column. We conclude that TSP1 contains a high-affinity binding site for polyhistidine and this is likely to be the molecular basis for the observed binding of TSP1 to histidine-rich glycoprotein. The possibility that other polyhistidine-containing proteins also interact with TSP1 warrants further study.

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6

Pogostin, Brett H., Anders Malmendal, Casey H. Londergan, and Karin S. Åkerfeldt. "pKa Determination of a Histidine Residue in a Short Peptide Using Raman Spectroscopy." Molecules 24, no. 3 (January 23, 2019): 405. http://dx.doi.org/10.3390/molecules24030405.

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Determining the pKa of key functional groups is critical to understanding the pH-dependent behavior of biological proteins and peptide-based biomaterials. Traditionally, 1H NMR spectroscopy has been used to determine the pKa of amino acids; however, for larger molecules and aggregating systems, this method can be practically impossible. Previous studies concluded that the C-D stretches in Raman are a useful alternative for determining the pKa of histidine residues. In this study, we report on the Raman application of the C2-D probe on histidine’s imidazole side chain to determining the pKa of histidine in a short peptide sequence. The pKa of the tripeptide was found via difference Raman spectroscopy to be 6.82, and this value was independently confirmed via 1H NMR spectroscopy on the same peptide. The C2-D probe was also compared to other Raman reporters of the protonation state of histidine and was determined to be more sensitive and reliable than other protonation-dependent signals. The C2-D Raman probe expands the tool box available to chemists interested in directly interrogating the pKa’s of histidine-containing peptide and protein systems.

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Liu, Yu, Huan-Huan Wan, Duo-Mei Tian, Xiao-Jun Xu, Chang-Long Bi, Xiao-Yong Zhan, Bi-Hui Huang, Yun-Sheng Xu, and Le-Ping Yan. "Development and Characterization of High Efficacy Cell-Penetrating Peptide via Modulation of the Histidine and Arginine Ratio for Gene Therapy." Materials 14, no. 16 (August 19, 2021): 4674. http://dx.doi.org/10.3390/ma14164674.

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Cell-penetrating peptides (CPPs), as non-viral gene delivery vectors, are considered with lower immunogenic response, and safer and higher gene capacity than viral systems. In our previous study, a CPP peptide called RALA (arginine rich) presented desirable transfection efficacy and owns a potential clinic use. It is believed that histidine could enhance the endosome escaping ability of CPPs, yet RALA peptide contains only one histidine in each chain. In order to develop novel superior CPPs, by using RALA as a model, we designed a series of peptides named HALA (increased histidine ratio). Both plasmid DNA (pDNA) and siRNA transfection results on three cell lines revealed that the transfection efficacy is better when histidine replacements were on the C-terminal instead of on the N-terminal, and two histidine replacements are superior to three. By investigating the mechanism of endocytosis of the pDNA nanocomplexes, we discovered that there were multiple pathways that led to the process and caveolae played the main role. During the screening, we discovered a novel peptide-HALA2 of high cellular transfection efficacy, which may act as an exciting gene delivery vector for gene therapy. Our findings also bring new insights on the development of novel robust CPPs.

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Zhang, Tong, Baoying Shen, and Xinghua Shi. "“Crawling” on the self-assembly system: A molecular simulation of peptide position adjusting over self-assembly block." MATEC Web of Conferences 189 (2018): 02002. http://dx.doi.org/10.1051/matecconf/201818902002.

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By combining non-equilibrium molecular dynamics(NEMD), umbrella sampling, and weighted histogram analysis method(WHAM), we calculated the potential of mean force of histidine peptide moving over a self-assembly structure. The reaction coordinate is along the main chain direction of the histidine peptide in the self-assembly structure. It is found that the energy needed for the histidine peptide with 3 and 5 residues while moving along the reaction coordinate is around -2.2 kCal/mol and -7.4 kCal/mol, respectively. And the histidine peptide crawls along the reaction coordinate, performing a snake-like movement. This result could illustrate how histidine peptide adjusts its position during self-assembly process.

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9

Lihi, Norbert, Daniele Sanna, István Bányai, Katalin Várnagy, and Imre Sóvágó. "Unusual binding modes in the copper(ii) and palladium(ii) complexes of peptides containing both histidyl and cysteinyl residues." New Journal of Chemistry 41, no. 3 (2017): 1372–79. http://dx.doi.org/10.1039/c6nj03735f.

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10

Tse, Dicky Lai-Yin, Ronald Ting-Kai Pang, Anderson On-Lam Wong, Siu-Ming Chan, Hubert Vaudry, and Billy Kwok-Chong Chow. "Identification of a Potential Receptor for Both Peptide Histidine Isoleucine and Peptide Histidine Valine." Endocrinology 143, no. 4 (April 1, 2002): 1327–36. http://dx.doi.org/10.1210/endo.143.4.8714.

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Abstract Peptide histidine isoleucine (PHI), peptide histidine valine (PHV), and vasoactive intestinal polypeptide (VIP) are cosynthesized from the same precursor and share high levels of structural similarities with overlapping biological functions. In this study, the first PHI/PHV receptor was isolated and characterized in goldfish. To study this receptor using homologous peptides, we have also characterized the goldfish prepro-PHI/VIP, and, surprisingly, a shorter transcript lacking the VIP coding region was isolated. A PHI/VIP precursor without the VIP coding sequence has never before been reported. Initial functional expression of the PHI/PHV receptor in Chinese hamster ovary cells revealed that it could be activated by human PHV [50% effective concentration (EC50): 43 nm] and to a lesser extent human PHI (EC50: 133 nm) and helodermin (EC50: 166 nm) but not fish and mammalian pituitary adenylate cyclase-activating polypeptides and VIPs. Subsequent studies indicated that, similar to the pituitary adenylate cyclase-activating polypeptide receptors (PAC1-R, VPAC1-R, and VPAC2-R), the receptor isolated in this study is able to interact with goldfish PHI and its C-terminally extended form, PHV with EC50 values 93 and 43 nm, respectively. Northern blot and RT-PCR/Southern blot analyses revealed that the PHI/VIP gene is expressed in the intestine, brain, and gall bladder and the PHI/PHV receptor gene is primarily expressed in the pituitary and to a lesser extend in the intestine and gall bladder, suggesting that PHI/PHV may play a role, notably in the regulation of pituitary function. In conclusion, our results demonstrate for the first time the existence of a PHI/PHV receptor, indicating that the functions of PHI and PHV could be mediated by their own receptor in addition to VIP receptors.

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11

Zhang, Shuyu, Liu Dong, Zhijie Bao, and Songyi Lin. "C-Terminal Modification on the Immunomodulatory Activity, Antioxidant Activity, and Structure–Activity Relationship of Pulsed Electric Field (PEF)-Treated Pine Nut Peptide." Foods 11, no. 17 (August 31, 2022): 2649. http://dx.doi.org/10.3390/foods11172649.

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In this study, a novel peptide VNAVL was synthesized by removing the C-terminal histidine on the basis of a bioactive peptide VNAVLH obtained from pine nut (Pinus koraiensis Sieb. et Zucc) protein. The effects of removing histidine on antioxidant activity, immunomodulatory activity, and secondary structure of the PEF-treated peptide were discussed. Compared with VNAVLH, VNAVL only exhibited lower antioxidant activity, but no immunomodulatory activity to release TNF-α, IL-6, and NO by activating RAW 264.7 cells. In addition, both antioxidant and immune activities of VNAVLH were significantly more sensitive to treatment with 40 kV/cm than other field intensities, whereas VNAVL was not sensitive to field strength changes. CD spectra and DSSP analysis verified that both peptides consisted of a β structure and random coil, but the ability of VNAVL to transform the random coil via PEF treatment is weaker than that of VNAVLH. Therefore, PEF treatment might expose the key active site located on the C-terminal histidine by altering the secondary structure of the peptide.

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12

Meena, Chhuttan L., Shubdha Ingole, Satyendra Rajpoot, Avinash Thakur, Prajwal P. Nandekar, Abhay T. Sangamwar, Shyam S. Sharma, and Rahul Jain. "Discovery of a low affinity thyrotropin-releasing hormone (TRH)-like peptide that exhibits potent inhibition of scopolamine-induced memory impairment in mice." RSC Advances 5, no. 70 (2015): 56872–84. http://dx.doi.org/10.1039/c5ra06935a.

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13

Watanobe, Hajime, Shinsuke Sasaki, and Kazuo Takebe. "Failure to confirm a growth hormone-releasing activity of corticotropin-releasing hormone in acromegaly: Comparison with the effects of other hypothalamic hormones." Acta Endocrinologica 125, no. 5 (November 1991): 487–90. http://dx.doi.org/10.1530/acta.0.1250487.

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Abstract. We re-examined whether CRH stimulates GH secretion in acromegaly. Human CRH (100 μg) was given as an iv bolus to 15 patients with active acromegaly, and plasma GH levels were measured before and at intervals up to 120 min after the injection. For comparison, we assessed in all the patients the effects of TRH (500 μg), GnRH (100 μg), vasoactive intestinal peptide (100 μg) and peptide histidine methionine (100 μg), which are known paradoxically to stimulate GH secretion in acromegaly. A paradoxical GH response (>50% above the basal) to TRH, GnRH, vasoactive intestinal peptide and peptide histidine methionine was observed in 12 (80%), 4 (27%), 5 (33%) and 2 (13%) patients, respectively. All the patients were responsive to at least one of these 4 peptides. However, none of the patients showed a positive GH response to hCRH. These results do not support a GH-releasing activity of CRH in acromegaly. Even if CRH has such an effect, it does not appear as potent as TRH, GnRH, vasoactive intestinal peptide and peptide histidine methionine. However, the possibility cannot be excluded that our negative data might have been due to the use of hCRH vs ovine CRH in earlier studies.

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Kagenishi, Tomoko, Ken Yokawa, Takashi Kadono, Kazuya Uezu, and Tomonori Kawano. "Copper-Binding Peptides from Human Prion Protein and Newly Designed Peroxidative Biocatalysts." Zeitschrift für Naturforschung C 66, no. 3-4 (April 1, 2011): 182–90. http://dx.doi.org/10.1515/znc-2011-3-413.

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A previous work suggested that peptides from the histidine-containing copper-binding motifs in human prion protein (PrP) function as peroxidase-like biocatalysts catalyzing the generation of superoxide anion radicals in the presence of neurotransmitters (aromatic monoamines) and phenolics such as tyrosine and tyrosyl residues on proteins. In this study, using various phenolic substrates, the phenol-dependent superoxide-generating activities of PrP-derived peptide sequences were compared. Among the peptides tested, the GGGTH pentapeptide was shown to be the most active catalyst for phenol-dependent reactions. Based on these results, we designed a series of oligoglycyl-histidines as novel peroxidative biocatalysts, and their catalytic performances including kinetics, heat tolerance, and freezing tolerance were analysed

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Huang, Kai-Jin, Yi-Chen Huang, and Yuya A. Lin. "Synthesis of Histidine-Containing Oligopeptides via Histidine-Promoted Peptide Ligation." Chemistry - An Asian Journal 13, no. 4 (February 1, 2018): 400–403. http://dx.doi.org/10.1002/asia.201701802.

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Kimura, Atsushi, Tadashi Arai, Miho Ueno, Kotaro Oyama, Hao Yu, Shinichi Yamashita, Yudai Otome, and Mitsumasa Taguchi. "Synthesis of Small Peptide Nanogels Using Radiation Crosslinking as a Platform for Nano-Imaging Agents for Pancreatic Cancer Diagnosis." Pharmaceutics 14, no. 11 (November 7, 2022): 2400. http://dx.doi.org/10.3390/pharmaceutics14112400.

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Nanoparticle-based drug delivery systems (DDS) have been developed as effective diagnostic and low-dose imaging agents. Nano-imaging agents with particles greater than 100 nm are difficult to accumulate in pancreatic cancer cells, making high-intensity imaging of pancreatic cancer challenging. Peptides composed of histidine and glycine were designed and synthesized. Additionally, aqueous peptide solutions were irradiated with γ-rays to produce peptide nanogels with an average size of 25–53 nm. The mechanisms underlying radiation-mediated peptide crosslinking were investigated by simulating peptide particle formation based on rate constants. The rate constants for reactions between peptides and reactive species produced by water radiolysis were measured using pulse radiolysis. HGGGHGGGH (H9, H—histidine; G—glycine) particles exhibited a smaller size, as well as high formation yield, stability, and biodegradability. These particles were labeled with fluorescent dye to change their negative surface potential and enhance their accumulation in pancreatic cancer cells. Fluorescent-labeled H9 particles accumulated in PANC1 human pancreatic cancer cells, demonstrating that these particles are effective nano-imaging agents for intractable cancers.

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Armstrong, K. M., and R. L. Baldwin. "Charged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone charges." Proceedings of the National Academy of Sciences 90, no. 23 (December 1, 1993): 11337–40. http://dx.doi.org/10.1073/pnas.90.23.11337.

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To determine whether a charged histidine side chain affects alpha-helix stability only when histidine is close to one end of the helix or also when it is in the central region, we substitute a single histidine residue at many positions in two reference peptides and measure helix stability and histidine pKa. The position of a charged histidine residue has a major effect on helix stability in 0.01 M NaCl: the helix content of a 17-residue peptide is 24% when histidine is at position 3 compared to 76% when it is at position 17. This dependence of helix content on histidine position decreases sharply in 1 M NaCl, as expected for counterion screening of the charge-helix dipole interaction. Results at interior positions indicate that the position of a charged histidine residue affects helix stability at these positions. Unexpectedly high values of the helix content are found when either neutral or charged histidine is at one of the last three C-terminal positions, suggesting that either form can stabilize an isolated helix by hydrogen bonding to a main-chain CO group.

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Nilsson, Jonas, Kerstin S. Broo, Richard S. Sott, and Lars Baltzer. "Article." Canadian Journal of Chemistry 77, no. 5-6 (June 1, 1999): 990–96. http://dx.doi.org/10.1139/v99-103.

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Peptides with 42 amino acid residues have been designed to fold into helix-loop-helix motifs that dimerize to form four-helix bundles and catalyze the hydrolysis of p-nitrophenyl esters. Their reactivities depend on nucleophilic and general-acid catalysis by cooperative HisH+-His pairs. The peptide catalyst MNV with the HisH+-His pair separated by three residues within the helical segment catalyzes the hydrolysis of p-nitrophenyl fumarate with a second-order rate constant of 0.034 M-1 s-1 at pH 5.1 and 290 K. This i, i+3 site is a factor of three more efficient than the corresponding i, i+4 site. Helix-loop-helix peptides having histidines situated at opposing helices were designed and exhibited cooperative HisH+-His catalytic pairs. The peptide H11,34K hydrolyzed p-nitrophenyl acetate and p-nitrophenyl valerate with second-order rate constants of 0.044 and 0.15 M-1 s-1, respectively, at pH 5.1 and 290 K, indicating that the hydrophobic substituent was recognized by the catalyst.Key words: de novo design, helix-loop-helix, four-helix bundle, histidine, catalysis.

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Dong, Na, Chensi Wang, Tingting Zhang, Lei Zhang, Chenyu Xue, Xinjun Feng, Chongpeng Bi, and Anshan Shan. "Bioactivity and Bactericidal Mechanism of Histidine-Rich β-Hairpin Peptide Against Gram-Negative Bacteria." International Journal of Molecular Sciences 20, no. 16 (August 14, 2019): 3954. http://dx.doi.org/10.3390/ijms20163954.

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Antibacterial peptides (APMs) are a new type of antibacterial substance. The relationship between their structure and function remains indistinct; in particular, there is a lack of a definitive and fixed template for designing new antimicrobial peptides. Previous studies have shown that porcine Protegrin-1 (PG-1) exhibits considerable antimicrobial activity and cytotoxicity. In this study, to reduce cytotoxicity and increase cell selectivity, we designed histidine-rich peptides based on the sequence template RR(XY)2XDPGX(YX)2RR-NH2, where X represents I, W, V, and F. The results showed that the peptides form more β-hairpin structures in a lipid-rich environment that mimics cell membranes. Among them, the antimicrobial peptide HV2 showed strong antibacterial activity against Gram-negative strains and almost no toxicity to normal cells. The results of our analysis of its antibacterial mechanism showed that peptide HV2 acts on the bacterial cell membrane to increase its permeability, resulting in cell membrane disruption and death. Furthermore, peptide HV2 inhibited bacterial movement in a concentration-dependent manner and had a more robust anti-inflammatory effect by inhibiting the production of TNF-α. In summary, peptide HV2 exhibits high bactericidal activity and cell selectivity, making it a promising candidate for future use as an antibiotic.

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Amirkhanov, N. V., A. V. Bardasheva, N. V. Tikunova, and D. V. Pyshnyi. "Synthetic Antimicrobial Peptides: III—Effect of Cationic Groups of Lysine, Arginine, and Histidine on Antimicrobial Activity of Peptides with a Linear Type of Amphipathicity." Russian Journal of Bioorganic Chemistry 47, no. 3 (May 2021): 681–90. http://dx.doi.org/10.1134/s106816202103002x.

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Abstract We have studied the antimicrobial and hemolytic activity of synthetic antimicrobial peptides (SAMPs), i.e., Arg9Phe2 (P1-Arg), Lys9Phe2 (P2-Lys), and His9Phe2 (P3-His), which have a “linear” type of amphipathicity and contain the cationic amino acid residues of arginine, lysine, or histidine. In this study, we have used various pathogenic microorganism strains of gram-negative bacteria (Pseudomonas aeruginosa, Escherichia coli, and Salmonella enterica), gram-positive bacteria (Staphylococcus aureus), and the conditionally pathogenic yeast fungus (Candida albicans). It has been shown that the replacement of the arginine residues by lysine or histidine residues in the tested SAMPs significantly degrades their antibacterial properties in the series: P1-Arg > P2-Lys $$ \gg $$P3-His. The cationic analog of SAMP, P1-Arg, has the highest antibacterial activity (MIC50 = 43–76 μM), while peptide P3-His does not exhibit this activity (MIC50 > 100 μM). The P1-Arg and P2-Lys peptides were 6–10 times more active against the opportunistic fungus C. albicans (MIC50 6.7 and 10.9 μM, respectively) and the P3-His peptide has 100-times increased antimycotic activity (MIC50 0.6 μM) compared with their effect on bacterial cells. All of the tested peptides with the linear type of amphipathicity and low hydrophobicity, i.e., P1-Arg, P2-Lys, and P3-His, that contain only two Phe residues regardless of the presence of cationic amino acids (Arg, Lys, or His) exhibit a relatively low hemolytic activity (not more than 4% hemolysis at 1000 μM peptide concentration). Thus, considering the same synthesis efficiency (56–63%) and approximately the same low toxicity of the tested SAMPs with a linear type of amphipathicity, it is recommended to use those that contain the cationic arginine or histidine residues to create antibacterial or antifungal peptide agents, respectively.

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Thom, S., A. Hughes, G. Martin, and P. S. Sever. "Endothelium-dependent relaxation in isolated human arteries and veins." Clinical Science 73, no. 5 (November 1, 1987): 547–52. http://dx.doi.org/10.1042/cs0730547.

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1. The role of the endothelium in mediating relaxation to acetylcholine, the calcium ionophore A23187, vasoactive intestinal peptide and peptide histidine methionine was studied using isolated human blood vessels. 2. Segments of renal, colic, pulmonary, uterine, transverse cervical, brachial, coronary and coeliac branch arteries, and saphenous veins, were obtained from surgical resection material for use in tissue bath studies. 3. Acetylcholine or A23187 produced endothelium-dependent relaxation in isolated vessels from all vascular beds studied. Coronary arteries, however, differed in their response to acetylcholine which produced predominantly a contractile response, either alone or after initial relaxation. 4. Vasoactive intestinal peptide and peptide histidine methionine produced endothelium-dependent relaxation in coeliac branch arteries. However, these peptides relaxed isolated pulmonary arteries independently of endothelium. 5. Endothelium-dependent relaxation in response to acetylcholine and A23187 was antagonized by nordihydroguaretic acid, a lipoxygenase inhibitor, and methylene blue and haemoglobin, inhibitors of soluble guanylate cyclase. In these respects the endothelium-dependent responses of human arteries to acetylcholine and A23187 resemble those described in other species.

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Mason, A. James, Claire Gasnier, Antoine Kichler, Gilles Prévost, Dominique Aunis, Marie-Hélène Metz-Boutigue, and Burkhard Bechinger. "Enhanced Membrane Disruption and Antibiotic Action against Pathogenic Bacteria by Designed Histidine-Rich Peptides at Acidic pH." Antimicrobial Agents and Chemotherapy 50, no. 10 (October 2006): 3305–11. http://dx.doi.org/10.1128/aac.00490-06.

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ABSTRACT The histidine-rich amphipathic cationic peptide LAH4 has antibiotic and DNA delivery capabilities. Here, we explore the interaction of peptides from this family with model membranes as monitored by solid-state 2H nuclear magnetic resonance and their antibiotic activities against a range of bacteria. At neutral pH, the membrane disruption is weak, but at acidic pH, the peptides strongly disturb the anionic lipid component of bacterial membranes and cause bacterial lysis. The peptides are effective antibiotics at both pH 7.2 and pH 5.5, although the antibacterial activity is strongly affected by the change in pH. At neutral pH, the LAH peptides were active against both methicillin-resistant and -sensitive Staphylococcus aureus strains but ineffective against Pseudomonas aeruginosa. In contrast, the LAH peptides were highly active against P. aeruginosa in an acidic environment, as is found in the epithelial-lining fluid of cystic fibrosis patients. Our results show that modest antibiotic activity of histidine-rich peptides can be dramatically enhanced by inducing membrane disruption, in this case by lowering the pH, and that histidine-rich peptides have potential as future antibiotic agents.

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Rzeszotarska, Barbara, and Elzbieta Masiukiewicz. "ARGININE, HISTIDINE AND TRYPTOPHAN IN PEPTIDE SYNTHESIS. THE IMIDAZOLE FUNCTION OF HISTIDINE." Organic Preparations and Procedures International 21, no. 4 (August 1989): 393–450. http://dx.doi.org/10.1080/00304948909356412.

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Myllylä, R., V. Günzler, K. I. Kivirikko, and D. D. Kaska. "Modification of vertebrate and algal prolyl 4-hydroxylases and vertebrate lysyl hydroxylase by diethyl pyrocarbonate. Evidence for histidine residues in the catalytic site of 2-oxoglutarate-coupled dioxygenases." Biochemical Journal 286, no. 3 (September 15, 1992): 923–27. http://dx.doi.org/10.1042/bj2860923.

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A search for conserved amino acid residues within the cDNA-derived amino acid sequences of 2-oxoglutarate-coupled dioxygenases revealed the presence of two distinct motifs, spaced 49-71 amino acids apart, toward the C-terminal regions of these proteins. Each of the two common motifs contains an invariant histidine residue at a conserved position. The 2-oxoglutarate-coupled dioxygenases function in diverse processes, including the post-translational hydroxylation of proline and lysine residues in vertebrate collagens and the biosynthesis of microbial cephalosporins, yet they have a common reaction mechanisms, which requires the binding of Fe2+, 2-oxoglutarate, O2 and ascorbate at the catalytic site. The two regions of homology, and specifically the identical histidines, potentially represent functionally important sites related to their catalytic activity. Modification of histidine residues by diethyl pyrocarbonate inactivated vertebrate and algal prolyl 4-hydroxylase and vertebrate lysyl hydroxylase, indicating that histidine residues function in the catalytic site of these 2-oxoglutarate-coupled dioxygenases. Inactivation was prevented by the presence of co-substrates, but not by the peptide substrate. It is proposed that the histidine residues in the conserved motifs may function as Fe(2+)-binding ligands.

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SAKATA, Kazuko, Toshihide YAMASHITA, Mitsuyo MAEDA, Yoshinori MORIYAMA, Shoichi SHIMADA, and Masaya TOHYAMA. "Cloning of a lymphatic peptide/histidine transporter." Biochemical Journal 356, no. 1 (May 15, 2001): 53. http://dx.doi.org/10.1042/0264-6021:3560053.

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SAKATA, Kazuko, Toshihide YAMASHITA, Mitsuyo MAEDA, Yoshinori MORIYAMA, Shoichi SHIMADA, and Masaya TOHYAMA. "Cloning of a lymphatic peptide/histidine transporter." Biochemical Journal 356, no. 1 (May 8, 2001): 53–60. http://dx.doi.org/10.1042/bj3560053.

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Although peptide transport across the plasma membrane has been characterized well in the kidney and the intestine, the functional relevance of this transport in other organs has not been addressed. Here we report the cloning of a cDNA for a novel peptide/histidine transporter found in the rat (rPHT2), whose mRNA is expressed mainly in the lymphatic system. rPHT2 encodes a protein of 582 amino acids and showed 49% identity with the brain PHT (PHT1) [Yamashita, Shimada, Guo, Sato, Kohmura, Hayakawa, Takagi and Tohyama (1997) J. Biol. Chem. 272, 10205–10211]. rPHT2 mRNA was abundant in lung, spleen and thymus, and detected faintly in brain, liver, adrenal gland and heart by Northern-blot analysis and reverse transcriptase PCR (RT-PCR). Intense signals for the gene were found in immunocytes using in situ hybridization. Ectopic expression of rPHT2 protein in HEK-293T cells and BHK cells was not found on the cell surface, but was found on the lysosomal membrane using light- and electron-microscopic analysis. Recombinant rPHT2 protein reconstituted into liposomes showed proton-dependent transport activity with histidine and histidyl-leucine. These findings suggest that rPHT2 is involved in the protein catabolic pathway in the lymphatic system.

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Calam, John, Yiangos Yiangou, Bobbie Chrysanthou, George Paul, Anand Mehta, and Stephen R. Bloom. "Peptide histidine methionine (PHM) increases ileostomy output." Regulatory Peptides 23, no. 1 (October 1988): 57–62. http://dx.doi.org/10.1016/0167-0115(88)90421-1.

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Pachter, J. A., D. W. Marshak, D. M. K. Lam, and K. R. Fry. "A peptide histidine isoleucine/peptide histidine methionine-like peptide in the rabbit retina: Colocalization with vasoactive intestinal peptide, synaptic relationships and activation of adenylate cyclase activity." Neuroscience 31, no. 2 (January 1989): 507–19. http://dx.doi.org/10.1016/0306-4522(89)90393-x.

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Song, Su Jeong, and Joon Sig Choi. "Enzyme-Responsive Amphiphilic Peptide Nanoparticles for Biocompatible and Efficient Drug Delivery." Pharmaceutics 14, no. 1 (January 7, 2022): 143. http://dx.doi.org/10.3390/pharmaceutics14010143.

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Self-assembled peptide nanostructures recently have gained much attention as drug delivery systems. As biomolecules, peptides have enhanced biocompatibility and biodegradability compared to polymer-based carriers. We introduce a peptide nanoparticle system containing arginine, histidine, and an enzyme-responsive core of repeating GLFG oligopeptides. GLFG oligopeptides exhibit specific sensitivity towards the enzyme cathepsin B that helps effective controlled release of cargo molecules in the cytoplasm. Arginine can induce cell penetration, and histidine facilitates lysosomal escape by its buffering capacity. Herein, we propose an enzyme-responsive amphiphilic peptide delivery system (Arg-His-(Gly-Phe-Lue-Gly)3, RH-(GFLG)3). The self-assembled RH-(GFLG)3 globular nanoparticle structure exhibited a positive charge and formulation stability for 35 days. Nile Red-tagged RH-(GFLG)3 nanoparticles showed good cellular uptake compared to the non-enzyme-responsive control groups with d-form peptides (LD (LRH-D(GFLG)3), DL (DRH-L(GFLG)3), and DD (DRH-D(GFLG)3). The RH-(GFLG)3 nanoparticles showed negligible cytotoxicity in HeLa cells and human RBCs. To determine the drug delivery efficacy, we introduced the anticancer drug doxorubicin (Dox) in the RH-(GFLG)3 nanoparticle system. LL-Dox exhibited formulation stability, maintaining the physical properties of the nanostructure, as well as a robust anticancer effect in HeLa cells compared to DD-Dox. These results indicate that the enzyme-sensitive RH-(GFLG)3 peptide nanoparticles are promising candidates as drug delivery carriers for biomedical applications.

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30

Terada, Tomohiro, Kyoko Sawada, Hideyuki Saito, Yukiya Hashimoto, and Ken-Ichi Inui. "Functional characteristics of basolateral peptide transporter in the human intestinal cell line Caco-2." American Journal of Physiology-Gastrointestinal and Liver Physiology 276, no. 6 (June 1, 1999): G1435—G1441. http://dx.doi.org/10.1152/ajpgi.1999.276.6.g1435.

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The apical H+-coupled peptide transporter (PEPT1) and basolateral peptide transporter in human intestinal Caco-2 cells were functionally compared by the characterization of [14C]glycylsarcosine transport. The glycylsarcosine uptake via the basolateral peptide transporter was less sensitive to medium pH than uptake via PEPT1 and was not transported against the concentration gradient. Kinetic analysis indicated that glycylsarcosine uptake across the basolateral membranes was apparently mediated by a single peptide transporter. Small peptides and β-lactam antibiotics inhibited glycylsarcosine uptake by the basolateral peptide transporter, and these inhibitions were revealed to be competitive. Comparison of the inhibition constant values of various β-lactam antibiotics between PEPT1 and the basolateral peptide transporter suggested that the former had a higher affinity than the latter. A histidine residue modifier, diethyl pyrocarbonate, inhibited glycylsarcosine uptake by both transporters, although the inhibitory effect was greater on PEPT1. These findings suggest that a single facilitative peptide transporter is expressed at the basolateral membranes of Caco-2 cells and that PEPT1 and the basolateral peptide transporter cooperate in the efficient transepithelial transport of small peptides and peptidelike drugs.

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Jayawardena, Bhawantha M., Lorraine Peacey, Roland Gamsjaeger, and Christopher E. Jones. "Essential Role of Histidine for Rapid Copper(II)-Mediated Disassembly of Neurokinin B Amyloid." Biomolecules 12, no. 11 (October 28, 2022): 1585. http://dx.doi.org/10.3390/biom12111585.

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Neurokinin B is a tachykinin peptide involved in a diverse range of neuronal functions. It rapidly forms an amyloid, which is considered physiologically important for efficient packing into dense core secretory vesicles within hypothalamic neurons. Disassembly of the amyloid is thought to require the presence of copper ions, which interact with histidine at the third position in the peptide sequence. However, it is unclear how the histidine is involved in the amyloid structure and why copper coordination can trigger disassembly. In this work, we demonstrate that histidine contributes to the amyloid structure via π-stacking interactions with nearby phenylalanine residues. The ability of neurokinin B to form an amyloid is dependent on any aromatic residue at the third position in the sequence; however, only the presence of histidine leads to both amyloid formation and rapid copper-induced disassembly.

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Chan, Kiat Hwa, Jaehong Lim, Joo Eun Jee, Jia Hui Aw, and Su Seong Lee. "Peptide–Peptide Co-Assembly: A Design Strategy for Functional Detection of C-peptide, A Biomarker of Diabetic Neuropathy." International Journal of Molecular Sciences 21, no. 24 (December 18, 2020): 9671. http://dx.doi.org/10.3390/ijms21249671.

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Diabetes-related neuropathy is a debilitating condition that may be averted if it can be detected early. One possible way this can be achieved at low cost is to utilise peptides to detect C-peptide, a biomarker of diabetic neuropathy. This depends on peptide-peptide co-assembly, which is currently in a nascent stage of intense study. Instead, we propose a bead-based triple-overlay combinatorial strategy that can preserve inter-residue information during the screening process for a suitable complementary peptide to co-assemble with C-peptide. The screening process commenced with a pentapeptide general library, which revealed histidine to be an essential residue. Further screening with seven tetrapeptide focused libraries led to a table of self-consistent peptide sequences that included tryptophan and lysine at high frequencies. Three complementary nonapeptides (9mer com-peptides), wpkkhfwgq (Trp-D), kwkkhfwgq (Lys-D), and KWKKHFWGQ (Lys-L) (as a negative control) were picked from this table for co-assembly studies with C-peptide. Attenuated total reflectance Fourier transform infrared (ATR-FTIR) and circular dichroism (CD) spectroscopies were utilized to study inter-peptide interactions and changes in secondary structures respectively. ATR-FTIR studies showed that there is indeed inter-peptide interaction between C-peptide and the tryptophan residues of the 9mer com-peptides. CD studies of unaggregated and colloidal C-peptide with the 9mer com-peptides suggest that the extent of co-assembly of C-peptide with Trp-D is greatest, followed by Lys-D and Lys-L. These results are promising and indicate that the presented strategy is viable for designing and evaluating longer complementary peptides, as well as complementary peptides for co-assembly with other polypeptides of interest and importance. We discuss the possibility of designing complementary peptides to inhibit toxic amyloidosis with this approach.

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Radko, Sergey P., Svetlana A. Khmeleva, Dmitry N. Kaluzhny, Olga I. Kechko, Yana Y. Kiseleva, Sergey A. Kozin, Vladimir A. Mitkevich, and Alexander A. Makarov. "The English (H6R) Mutation of the Alzheimer’s Disease Amyloid-β Peptide Modulates Its Zinc-Induced Aggregation." Biomolecules 10, no. 6 (June 25, 2020): 961. http://dx.doi.org/10.3390/biom10060961.

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The coordination of zinc ions by histidine residues of amyloid-beta peptide (Aβ) plays a critical role in the zinc-induced Aβ aggregation implicated in Alzheimer’s disease (AD) pathogenesis. The histidine to arginine substitution at position 6 of the Aβ sequence (H6R, English mutation) leads to an early onset of AD. Herein, we studied the effects of zinc ions on the aggregation of the Aβ42 peptide and its isoform carrying the H6R mutation (H6R-Aβ42) by circular dichroism spectroscopy, dynamic light scattering, turbidimetric and sedimentation methods, and bis-ANS and thioflavin T fluorescence assays. Zinc ions triggered the occurrence of amorphous aggregates for both Aβ42 and H6R-Aβ42 peptides but with distinct optical properties. The structural difference of the formed Aβ42 and H6R-Aβ42 zinc-induced amorphous aggregates was also supported by the results of the bis-ANS assay. Moreover, while the Aβ42 peptide demonstrated an increase in the random coil and β-sheet content upon complexing with zinc ions, the H6R-Aβ42 peptide showed no appreciable structural changes under the same conditions. These observations were ascribed to the impact of H6R mutation on a mode of zinc/peptide binding. The presented findings further advance the understanding of the pathological role of the H6R mutation and the role of H6 residue in the zinc-induced Aβ aggregation.

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Kállay, Csilla, Zoltán Nagy, Katalin Várnagy, Gerasimos Malandrinos, Nick Hadjiliadis, and Imre Sóvágó. "Thermodynamic and Structural Characterization of the Copper(II) Complexes of Peptides Containing Both Histidyl and Aspartyl Residues." Bioinorganic Chemistry and Applications 2007 (2007): 1–9. http://dx.doi.org/10.1155/2007/30394.

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Terminally protected pentapeptides with 2 histidines (Ac-HHVGD-NH2and Ac-HVGDH-NH2) and the terminally free peptides containing both internal aspartyl and C-terminal histidyl residues (FDAH and VIDAH) have been synthesized, and copper(II) complexes studied by potentiometric, UV-Vis, CD, and EPR spectroscopic techniques in solution. Both thermodynamic and spectroscopic data reveal that side chain donor atoms of aspartyl and histidyl residues have a significant contribution to the metal binding affinity of peptide molecules. In the case of terminally protected peptides, the role of the imidazole-N donor functions is reflected in the enhanced stability of the 3N and 4N coordinated copper(II) complexes. The amino andβ-carboxylate groups of FDAH and VIDAH create a very effective metal binding site with the (NH2,N−,β-COO−) and (NH2,N−,N−,β-COO−) coordination modes including the N-termini, while the histidine sites are available for the formation of the (Nim,N−,N−) binding mode resulting in the preference of dinuclear complex formation.

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35

Wittmann-Liebold, Brigitte, Monika Ühlein, Henning Urlaub, Eva-Christina Müller, Albrecht Otto, and Oliver Bischof. "Structural and functional implications in the eubacterial ribosome as revealed by protein–rRNA and antibiotic contact sites." Biochemistry and Cell Biology 73, no. 11-12 (December 1, 1995): 1187–97. http://dx.doi.org/10.1139/o95-128.

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Contact sites between protein and rRNA in 30S and 50S ribosomal subunits of Escherichia coli and Bacillus stearothermophilus were investigated at the molecular level using UV and 2–iminothiolane as cross-linkers. Thirteen ribosomal proteins (S3, S4, S7, S14, S17, L2, L4, L6, L14, L27, L28, L29, andL36) from these organisms were cross-linked in direct contact with the RNAs, and the peptide stretches as well as amino acids involved were identified. Further, the binding sites of puromycin and spiramycin were established at die peptide level in several proteins that were found to constitute me antibiotic-binding sites. Peptide stretches of puromycin binding were identified from proteins S7, S14, S18, L18, and L29; those of spiramycin attachment were derived from proteins S12, S14, L17, L18, L27, and L35. Comparison of the RNA–peptide contact sites with the peptides identified for antibiotic binding and with those altered in antibiotic-resistant mutants clearly showed identical peptide areas to be involved and, hence, demonstrated the functional importance of these peptides. Further evidence for a functional implication of ribosomal proteins in the translational process came from complementation experiments in which protein L2 from Halobacterium marismortui was incorporated into the E. coli ribosomes that were active. The incorporated protein was present in 50S subunits and 70S particles, in disomes, and in higher polysomes. These results clearly demonstrate the functional implication of protein L2 in protein biosynthesis. Incorporation studies with a mutant of HmaL2 widi a replacement of histidine-229 by glycine completely abolished the functional activity of the ribosome. Accordingly, protein L2 with histidine-229 is a crucial element of the translational machinery.Key words: antibiotic-binding site, RNA–peptide-binding sites, protein–RNA interaction in ribosomes, functional role of protein L2.

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36

Saha, Abhik, Archna Sharma, Amlanjyoti Dhar, Bhabatarak Bhattacharyya, Siddhartha Roy, and Sujoy K. Das Gupta. "Antagonists of Hsp16.3, a Low-Molecular-Weight Mycobacterial Chaperone and Virulence Factor, Derived from Phage-Displayed Peptide Libraries." Applied and Environmental Microbiology 71, no. 11 (November 2005): 7334–44. http://dx.doi.org/10.1128/aem.71.11.7334-7344.2005.

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ABSTRACT The persistence of Mycobacterium tuberculosis is a major cause of concern in tuberculosis (TB) therapy. In the persistent mode the pathogen can resist drug therapy, allowing the possibility of reactivation of the disease. Several protein factors have been identified that contribute to persistence, one of them being the 16-kDa low-molecular-weight mycobacterial heat shock protein Hsp16.3, a homologue of the mammalian eye lens protein alpha-crystallin. It is believed that Hsp16.3 plays a key role in the persistence phase by protecting essential proteins from being irreversibly denatured. Because of the close association of Hsp16.3 with persistence, an attempt has been made to develop inhibitors against it. Random peptide libraries displayed on bacteriophage M13 were screened for Hsp16.3 binding. Two phage clones were identified that bind to the Hsp16.3 protein. The corresponding synthetic peptides, an 11-mer and a 16-mer, were able to bind Hsp16.3 and inhibit its chaperone activity in vitro in a dose-dependent manner. Little or no effect of these peptides was observed on alphaB-crystallin, a homologous protein that is a key component of human eye lens, indicating that there is an element of specificity in the observed inhibition. Two histidine residues appear to be common to the selected peptides. Nuclear magnetic resonance studies performed with the 11-mer peptide indicate that in this case these two histidines may be the crucial binding determinants. The peptide inhibitors of Hsp16.3 thus obtained could serve as the basis for developing potent drugs against persistent TB.

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Afrose, Fahmida, and Roger E. Koeppe II. "Comparing Interfacial Trp, Interfacial His and pH Dependence for the Anchoring of Tilted Transmembrane Helical Peptides." Biomolecules 10, no. 2 (February 11, 2020): 273. http://dx.doi.org/10.3390/biom10020273.

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Charged and aromatic amino acid residues, being enriched toward the terminals of membrane-spanning helices in membrane proteins, help to stabilize particular transmembrane orientations. Among them, histidine is aromatic and can be positively charge at low pH. To enable investigations of the underlying protein-lipid interactions, we have examined the effects of single or pairs of interfacial histidine residues using the constructive low-dynamic GWALP23 (acetyl-GG2ALW5LALALALALALALW19LAG22A-amide) peptide framework by incorporating individual or paired histidines at locations 2, 5, 19 or 22. Analysis of helix orientation by means of solid-state 2H NMR spectra of labeled alanine residues reveals marked differences with H2,22 compared to W2,22. Nevertheless, the properties of membrane-spanning H2,22WALP23 helices show little pH dependence and are similar to those having Gly, Arg or Lys at positions 2 and 22. The presence of H5 or H19 influences the helix rotational preference but not the tilt magnitude. H5 affects the helical integrity, as residue 7 unwinds from the core helix; yet once again the helix orientation and dynamic properties show little sensitivity to pH. The overall results reveal that the detailed properties of transmembrane helices depend upon the precise locations of interfacial histidine residues.

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38

Holst, J. J., J. Fahrenkrug, S. Knuhtsen, S. L. Jensen, O. V. Nielsen, J. M. Lundberg, and T. Hokfelt. "VIP and PHI in the pig pancreas: coexistence, corelease, and cooperative effects." American Journal of Physiology-Gastrointestinal and Liver Physiology 252, no. 2 (February 1, 1987): G182—G189. http://dx.doi.org/10.1152/ajpgi.1987.252.2.g182.

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The human vasoactive intestinal polypeptide (VIP) precursor contains a sequence, a peptide with an N-terminal histidine and C-terminal methionine (PHM), which is 93% homologous to the porcine intestinal peptide, (PHI) a peptide having N-terminal histidine and C-terminal isoleucine amide, suggesting that PHI could be a product of the porcine VIP precursor. If so, VIP-producing nerves would be expected to produce and release PHI in addition to VIP. We studied this in the pig pancreas. By immunohistochemistry, we identified nerve cell bodies in local ganglia and nerve fibers that were both PHI and VIP immunoreactive, innervating exocrine as well as endocrine structures. During electrical stimulation of the vagus nerve supply to the isolated perfused pig pancreas, a synchronous and approximately equimolar release of immunoreactive PHI and VIP was observed. Both responses were abolished by hexamethonium and could be copied by cholinergic agonists. Infusions of PHI and VIP at 10(-9) M stimulated the exocrine secretion of fluid and bicarbonate, and the effect of a combination of the two peptides was additive. In addition, both peptides stimulated insulin as well as glucagon secretion. By gel chromatography the VIP immunoreactivity in the venous effluent corresponded precisely to synthetic VIP, but only 24% of the PHI immunoreactivity corresponded to synthetic PHI; a larger peptide (mol wt 5,000-7,000) was responsible for the majority. The biological activity of this component is unknown. The results suggest that both VIP and PHI, released from intrapancreatic nerve fibers, participate in the parasympathetic control of pancreatic secretion.

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Lee, Myungwoon, Tuo Wang, Olga V. Makhlynets, Yibing Wu, Nicholas F. Polizzi, Haifan Wu, Pallavi M. Gosavi, et al. "Zinc-binding structure of a catalytic amyloid from solid-state NMR." Proceedings of the National Academy of Sciences 114, no. 24 (May 31, 2017): 6191–96. http://dx.doi.org/10.1073/pnas.1706179114.

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Throughout biology, amyloids are key structures in both functional proteins and the end product of pathologic protein misfolding. Amyloids might also represent an early precursor in the evolution of life because of their small molecular size and their ability to self-purify and catalyze chemical reactions. They also provide attractive backbones for advanced materials. When β-strands of an amyloid are arranged parallel and in register, side chains from the same position of each chain align, facilitating metal chelation when the residues are good ligands such as histidine. High-resolution structures of metalloamyloids are needed to understand the molecular bases of metal–amyloid interactions. Here we combine solid-state NMR and structural bioinformatics to determine the structure of a zinc-bound metalloamyloid that catalyzes ester hydrolysis. The peptide forms amphiphilic parallel β-sheets that assemble into stacked bilayers with alternating hydrophobic and polar interfaces. The hydrophobic interface is stabilized by apolar side chains from adjacent sheets, whereas the hydrated polar interface houses the Zn2+-binding histidines with binding geometries unusual in proteins. Each Zn2+ has two bis-coordinated histidine ligands, which bridge adjacent strands to form an infinite metal–ligand chain along the fibril axis. A third histidine completes the protein ligand environment, leaving a free site on the Zn2+ for water activation. This structure defines a class of materials, which we call metal–peptide frameworks. The structure reveals a delicate interplay through which metal ions stabilize the amyloid structure, which in turn shapes the ligand geometry and catalytic reactivity of Zn2+.

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40

Bezrodnyi, Valeriy V., Sofia E. Mikhtaniuk, Oleg V. Shavykin, Igor M. Neelov, Nadezhda N. Sheveleva, and Denis A. Markelov. "Size and Structure of Empty and Filled Nanocontainer Based on Peptide Dendrimer with Histidine Spacers at Different pH." Molecules 26, no. 21 (October 29, 2021): 6552. http://dx.doi.org/10.3390/molecules26216552.

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Novel peptide dendrimer with Lys-2His repeating units was recently synthesized, studied by NMR (Molecules, 2019, 24, 2481) and tested as a nanocontainer for siRNA delivery (Int. J. Mol. Sci., 2020, 21, 3138). Histidine amino acid residues were inserted in the spacers of this dendrimer. Increase of their charge with a pH decrease turns a surface-charged dendrimer into a volume-charged one and should change all properties. In this paper, the molecular dynamics simulation method was applied to compare the properties of the dendrimer in water with explicit counterions at two different pHs (at normal pH with neutral histidines and at low pH with fully protonated histidines) in a wide interval of temperatures. We obtained that the dendrimer at low pH has essentially larger size and size fluctuations. The electrostatic properties of the dendrimers are different but they are in good agreement with the theoretical soft sphere model and practically do not depend on temperature. We have shown that the effect of pairing of side imidazole groups is much stronger in the dendrimer with neutral histidines than in the dendrimer with protonated histidines. We also demonstrated that the capacity of a nanocontainer based on this dendrimer with protonated histidines is significantly larger than that of a nanocontainer with neutral histidines.

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Djalali, Ramin, Yung-fou Chen, and Hiroshi Matsui. "Au Nanowire Fabrication from Sequenced Histidine-Rich Peptide." Journal of the American Chemical Society 124, no. 46 (November 2002): 13660–61. http://dx.doi.org/10.1021/ja028261r.

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Murakami, Yukitaka, Satoshi Shizukuishi, Akira Tsunemitsu, Kazuhisa Nakashima, Yukio Kato, and Saburo Aimoto. "Binding of a histidine-rich peptide toPorphyromonas gingivalis." FEMS Microbiology Letters 82, no. 3 (August 1991): 253–56. http://dx.doi.org/10.1111/j.1574-6968.1991.tb04890.x.

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43

Beyerman, H. C., J. Hirt, P. Kranenburg, J. L. M. Syrier, and A. van Zon. "Excess mixed anhydride peptide synthesis with histidine derivatives." Recueil des Travaux Chimiques des Pays-Bas 93, no. 9-10 (September 2, 2010): 256–57. http://dx.doi.org/10.1002/recl.19740930907.

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44

Stone, S. R., D. Rennex, P. Wikstrom, E. Shaw, and J. Hofsteenge. "Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of modification." Biochemical Journal 276, no. 3 (June 15, 1991): 837–40. http://dx.doi.org/10.1042/bj2760837.

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The kinetics of inactivation of prolyl endopeptidase by acetyl-Ala-Ala-Pro-CH2Cl were studied by progress-curve methods in the presence of substrate. The kinetic mechanism was found to involve the formation of an initial complex between the enzyme and the chloromethane followed by an inactivation step. The substrate was shown to compete for the formation of the initial complex, indicating that binding at the active site was a prerequisite for inactivation. After reaction of the enzyme with [3H]acetyl-Ala-Ala-Pro-CH2Cl, it was possible to isolate five labelled peptides. Four of these peptides contained a cysteine residue as the site of modification, whereas the fifth peptide contained no cysteine and a histidine residue was identified as the site of modification. This residue (His-680) probably represents the active-site histidine of prolyl endopeptidase.

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45

Campanelli, J. T., and R. H. Scheller. "Histidine-rich basic peptide: a cardioactive neuropeptide from Aplysia neurons R3-14." Journal of Neurophysiology 57, no. 4 (April 1, 1987): 1201–9. http://dx.doi.org/10.1152/jn.1987.57.4.1201.

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We have previously demonstrated that neurons R3-14 of the Aplysia abdominal ganglia specifically express a gene encoding a 108-amino acid neuropeptide precursor. This precursor is postranslationally processed by cleavage of a signal sequence and two internal dibasic residues resulting in three peptides. The peptide products are colocalized in dense core granules throughout the R3-14 processes that innervate the efferent vein of the gill and the auricle. Gel filtration and reverse phase high-pressure liquid chromatography (rpHPLC) were used to purify a 4.9-kDa peptide produced by the R3-14 neurons. We call this peptide the histidine-rich basic peptide (HRBP), which reflects its primary structure. In vitro tension measurements of cannulated Aplysia hearts revealed dose-dependent cardioexcitatory actions of HRBP. HRBP increased both beat frequency and amplitude with a threshold of 10(-7) M. HRBP increased the amplitude of ventricular contractions in a dose-dependent manner, whereas the frequency of contraction is unaffected. In contrast both the amplitude and frequency of auricular contractions were enhanced. High concentrations of HRBP also had a positive tonotropic effect on the auricle. HRBP was also demonstrated to have actions on tissue of the gut. Circular muscles of the crop adjacent to the anterior gizzard showed infrequent spontaneous contractions. Both HRBP and acetylcholine (ACh) induced repetitive contractions of this muscle. Circular muscles of the posterior gizzard had a high degree of spontaneous activity when continually perfused. Contraction amplitude and frequency was increased by HRBP and ACh, whereas contractility was inhibited by Phe-Met-Arg-Phe-amide (FMRFamide).

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Frenkel-Pinter, Moran, Alyssa B. Sargon, Jennifer B. Glass, Nicholas V. Hud, and Loren Dean Williams. "Transition metals enhance prebiotic depsipeptide oligomerization reactions involving histidine." RSC Advances 11, no. 6 (2021): 3534–38. http://dx.doi.org/10.1039/d0ra07965k.

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47

Tabata, Masaaki, and Bibudhendra Sarkar. "Kinetic mechanism of copper(II) transfer between the native sequence peptide representing the copper(II)-transport site of human serum albumin and L-histidine." Canadian Journal of Chemistry 63, no. 11 (November 1, 1985): 3111–16. http://dx.doi.org/10.1139/v85-513.

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The kinetics for Cu(II)-transfer reaction of the native sequence tripeptide, L-aspartyl-L-alanyl-L-histidine-N-methyl amide (AAHNMA), representing the Cu(II)-transport site of human serum albumin (HSA), and L-histidine (L-His) was studied in the forward and reverse reactions in a pH range 6.5–10.0 at I = 0.2 and 25°. For the Cu(II)-transfer from Cu(II)-L-His2 to native sequence peptide, the rate-determining step is a bond formation between Cu(II) and peptide nitrogen to form CuH−1AB from CuAB by deprotonation of peptide nitrogen atom, where A and B denote the anionic forms of AAHNMA and L-His, respectively. For the Cu(II)-transfer reaction from Cu(II)–peptide to L-His, the rate-determining step is a bond breaking between Cu(II) and peptide nitrogen to form CuAB fromCuH−1AB by protonation to a peptide nitrogen. The effect of carboxyl group of aspartyl residue in the native sequence peptide on the kinetic and equilibrium constants are discussed.

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Ravindran, Velmurugu, Patrick C. H. Morel, Shane M. Rutherfurd, and Donald V. Thomas. "Endogenous flow of amino acids in the avian ileum as influenced by increasing dietary peptide concentrations." British Journal of Nutrition 101, no. 6 (July 29, 2008): 822–28. http://dx.doi.org/10.1017/s0007114508039974.

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The aim of the present study was to establish whether feeding broiler chickens with diets containing increasing dietary peptide concentrations would cause increases in ileal endogenous amino acid flow. The flow of N and most amino acids increased quadratically (P < 0·05 to 0·001) with increasing dietary concentrations of peptides. The exceptions were the flow of threonine, serine, glycine, tyrosine and cystine, which increased linearly (P < 0·001) with dietary peptide levels. Another notable exception to the general trend was the flow of proline, which was significantly higher (P < 0·01) in birds fed the protein-free diet. The amino acid profile of endogenous protein, expressed as proportion of crude protein, indicated that the ratios of threonine, glutamic acid, proline, glycine, leucine, histidine, arginine and cystine were influenced (P < 0·05) with increasing dietary peptide concentrations. In general, compared with the protein-free diet, the ratios of threonine and arginine in endogenous protein were lower (P < 0·05) and those of glutamic acid, glycine and histidine were greater (P < 0·05) in diets with high concentrations of peptides. The ratio of proline was found to decrease (P < 0·05) with increasing dietary peptide concentrations. These changes in the amino acid profile of endogenous protein are probably reflective of changes in the output of one or more of the components of endogenous protein. Overall, the present results demonstrated that increasing dietary peptide concentrations increased the flow of endogenous amino acid flow at the terminal ileum of broiler chickens in a dose-dependent manner and also caused changes in the composition of endogenous protein. The observed changes in endogenous amino flow will influence the maintenance requirements for amino acids and also have implications for the calculation of true digestibility coefficient of feedstuffs.

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Yu, Hui-Yuan, Chih-Hsiung Tu, Bak-Sau Yip, Heng-Li Chen, Hsi-Tsung Cheng, Kuo-Chun Huang, Hsiu-Jung Lo, and Jya-Wei Cheng. "Easy Strategy To Increase Salt Resistance of Antimicrobial Peptides." Antimicrobial Agents and Chemotherapy 55, no. 10 (July 18, 2011): 4918–21. http://dx.doi.org/10.1128/aac.00202-11.

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ABSTRACTThe efficacies of many antimicrobial peptides are greatly reduced under high salt concentrations, limiting their development as pharmaceutical compounds. Here, we describe an easy strategy to increase salt resistance of antimicrobial peptides by replacing tryptophan or histidine residues with the bulky amino acids β-naphthylalanine and β-(4,4′-biphenyl)alanine. The activities of the salt-sensitive peptide P-113 were diminished at high salt concentrations, whereas the activities of its β-naphthylalanine and β-(4,4′-biphenyl)alanine-substituted variant were less affected.

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Yadav, Kranthikumar, J. Laxmikanth Rao, R. Srinivas, R. Nagaraj, and MV Jagannadham. "Characterization of acetylated histidine b1-ion structure: A competition between oxazolone and side chain imidazole moiety." European Journal of Mass Spectrometry 24, no. 3 (February 2, 2018): 261–68. http://dx.doi.org/10.1177/1469066718756801.

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The detection of post-translational modifications of proteins is an important comprehensive research area. Over the years, proteomic studies involving protein acetylation have attracted a great deal of attention. In the present study, we have focussed on the acetylation of histidine and the intrinsic stability of b1-ion of oxazolone ring and/or with side chain imidazole bicyclic product. The formation of oxazolone structure may occur when an amino moiety undergoes acetylation reaction and when it is present in the vicinity of the side chain imidazole moiety. Tryptic peptides generated from the proteins of Acenitobacter radioresistens MMC5-containing N-terminal histidine were explored in a standard proteomic workflow. Formation of [Formula: see text] ion with an oxazolone ring in these peptides has been supported by a tandem mass spectrometric study of a synthetic peptide and density functional theory calculations. The results obtained from this study have implications in understanding the fragmentation of the peptides generated in the proteomic workflows.

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Journal articles on the topic 'Histidine peptide'

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