Relevant bibliographies by topics / Peptides

Academic literature on the topic 'Peptides'

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Published: 4 June 2021
Last updated: 30 July 2024

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Journal articles on the topic "Peptides"

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Ng, Sandy Y. M., David J. VanDyke, Bonnie Chaban, John Wu, Yoshika Nosaka, Shin-Ichi Aizawa, and Ken F. Jarrell. "Different Minimal Signal Peptide Lengths Recognized by the Archaeal Prepilin-Like Peptidases FlaK and PibD." Journal of Bacteriology 191, no. 21 (August 28, 2008): 6732–40. http://dx.doi.org/10.1128/jb.00673-09.

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ABSTRACT In Archaea, the preflagellin peptidase (a type IV prepilin-like peptidase designated FlaK in Methanococcus voltae and Methanococcus maripaludis) is the enzyme that cleaves the N-terminal signal peptide from preflagellins. In methanogens and several other archaeal species, the typical flagellin signal peptide length is 11 to 12 amino acids, while in other archaea preflagellins possess extremely short signal peptides. A systematic approach to address the signal peptide length requirement for preflagellin processing is presented in this study. M. voltae preflagellin FlaB2 proteins with signal peptides 3 to 12 amino acids in length were generated and used as a substrate in an in vitro assay utilizing M. voltae membranes as an enzyme source. Processing by FlaK was observed in FlaB2 proteins containing signal peptides shortened to 5 amino acids; signal peptides 4 or 3 amino acids in length were unprocessed. In the case of Sulfolobus solfataricus, where the preflagellin peptidase PibD has broader substrate specificity, some predicted substrates have predicted signal peptides as short as 3 amino acids. Interestingly, the shorter signal peptides of the various mutant FlaB2 proteins not processed by FlaK were processed by PibD, suggesting that some archaeal preflagellin peptidases are likely adapted toward cleaving shorter signal peptides. The functional complementation of signal peptidase activity by FlaK and PibD in an M. maripaludis ΔflaK mutant indicated that processing of preflagellins was detected by complementation with either FlaK or PibD, yet only FlaK-complemented cells were flagellated. This suggested that a block in an assembly step subsequent to signal peptide removal occurred in the PibD complementation.
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Ito, Toshihiko, Yuki Taguchi, Haruka Oue, Naomi Amano, Yusuke Nagae, Koji Noge, and Katsumi Hashizume. "Formation of taste-active pyroglutamyl peptide ethyl esters in sake by rice koji peptidases." Bioscience, Biotechnology, and Biochemistry 85, no. 6 (March 15, 2021): 1476–84. http://dx.doi.org/10.1093/bbb/zbab041.

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ABSTRACT Formation of taste-active pyroglutamyl (pGlu) peptide ethyl esters in sake was investigated: 2 enzymes (A and B) responsible for the esterification were purified from a rice koji extract. MADLI-TOF/TOF analysis after deglycosylation identified enzyme (A) as peptidase S28 (GenBank accession number OOO13707.1) and enzyme (B) as serine-type carboxypeptidase (accession number AO090010000534). Both enzymes hydrolyzed pGlu peptides and formed ethyl esters under sake mash conditions: acidic pH (3-4) and in ethanol (5%-20% v/v) aqueous solutions. Enzyme (A) formed pGlu penta-peptide ethyl esters from pGlu undeca-peptides by a prolyl endo-type reaction. Enzyme (B) formed (pGlu) deca-peptide and its ethyl esters from pGlu undeca-peptides in an exo-type reaction. We are the first to report the enzymatic ethyl esterification reaction in the formation of pGlu peptides by rice koji peptidases.
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Liu, Yu, Jeffrey A. Sigman, Lisa A. Bruce, and Adele J. Wolfson. "Thimet Oligopeptidase—A Classical Enzyme with New Function and New Form." Immuno 1, no. 4 (September 23, 2021): 332–46. http://dx.doi.org/10.3390/immuno1040022.

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Peptidases generate bioactive peptides that can regulate cell signaling and mediate intercellular communication. While the processing of peptide precursors is initiated intracellularly, some modifications by peptidases may be conducted extracellularly. Thimet oligopeptidase (TOP) is a peptidase that processes neuroendocrine peptides with roles in mood, metabolism, and immune responses, among other functions. TOP also hydrolyzes angiotensin I to angiotensin 1–7, which may be involved in the pathophysiology of COVID-19 infection. Although TOP is primarily cytosolic, it can also be associated with the cell plasma membrane or secreted to the extracellular space. Recent work indicates that membrane-associated TOP can be released with extracellular vesicles (EVs) to the extracellular space. Here we briefly summarize the enzyme’s classical function in extracellular processing of neuroendocrine peptides, as well as its more recently understood role in intracellular processing of various peptides that impact human diseases. Finally, we discuss new findings of EV-associated TOP in the extracellular space.
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Nong, Nhung Thi Phuong, Christoper Caesar Yudho Sutopo, Wei-Ting Hung, Ping-Hsun Wu, and Jue-Liang Hsu. "The Molecular Docking and Inhibition Kinetics of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Soft-Shelled Turtle Yolk." Applied Sciences 12, no. 23 (December 2, 2022): 12340. http://dx.doi.org/10.3390/app122312340.

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The soft-shelled turtle yolk (SSTY) protein hydrolysate contains a potential source of bioactive peptides. Our previous study found that five SSTY peptides (WLQL, LPSW, LPLF, VPGLAL and LVGLPL) showed moderate to high dipeptidyl peptidase IV (DPP-IV) inhibitory activities. This study further investigated their angiotensin-I-converting enzyme (ACE) inhibitory activity. Consequently, WLQL was identified as the most potent ACE inhibitory peptide with a remarkably low IC50 value (16.87 ± 0.54 µM). The Lineweaver–Burk plot analysis was performed for the characterization of the peptide’s inhibition mode and the inhibition kinetics was rationalized using the molecular docking simulation. The result revealed that WLQL would dock into the S1 pockets of ACE, while LPSW interacted with ACE’s secondary binding site. Further evaluation of the peptides’ stability against ACE involved a pre-incubation experiment. After 3 h of pre-incubation with ACE, the four peptides were hydrolyzed into smaller fragments with varying degrees, suggesting that they are substrate-type inhibitors. In contrast, LVGLPL can tolerate hydrolysis by ACE and act as a true inhibitor.
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Tani, Naoki, Kohei Kazuma, Yukio Ohtsuka, Yasushi Shigeri, Keiichi Masuko, Katsuhiro Konno, and Hidetoshi Inagaki. "Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components." Toxins 11, no. 1 (January 17, 2019): 50. http://dx.doi.org/10.3390/toxins11010050.

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We previously identified 92 toxin-like peptides and proteins, including pilosulin-like peptides 1–6 from the predatory ant Odontomachus monticola, by transcriptome analysis. Here, to further characterize venom components, we analyzed the venom and venom sac extract by ESI-MS/MS with or without trypsin digestion and reducing agent. As the low-molecular-mass components, we found amino acids (leucine/isoleucine, phenylalanine, and tryptophan) and biogenic amines (histamine and tyramine) in the venom and venom sac extract. As the higher molecular mass components, we found peptides and proteins such as pilosulin-like peptides, phospholipase A2s, hyaluronidase, venom dipeptidyl peptidases, conotoxin-like peptide, and icarapin-like peptide. In addition to pilosulin-like peptides 1–6, we found three novel pilosulin-like peptides that were overlooked by transcriptome analysis. Moreover, pilosulin-like peptides 1–6 were chemically synthesized, and some of them displayed antimicrobial, hemolytic, and histamine-releasing activities.
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ANDERSON, John W., Suara A. ADEDIRAN, Paulette CHARLIER, Martine NGUYEN-DISTÈCHE, Jean-Marie FRÈRE, Robert A. NICHOLAS, and Rex F. PRATT. "On the substrate specificity of bacterial DD-peptidases: evidence from two series of peptidoglycan-mimetic peptides." Biochemical Journal 373, no. 3 (August 1, 2003): 949–55. http://dx.doi.org/10.1042/bj20030217.

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The reactions between bacterial DD-peptidases and β-lactam antibiotics have been studied for many years. Less well understood are the interactions between these enzymes and their natural substrates, presumably the peptide moieties of peptidoglycan. In general, remarkably little activity has previously been demonstrated in vitro against potential peptide substrates, although in many cases the peptides employed were non-specific and not homologous with the relevant peptidoglycan. In this paper, the specificity of a panel of DD-peptidases against elements of species-specific d-alanyl-d-alanine peptides has been assessed. In two cases, those of soluble, low-molecular-mass DD-peptidases, high activity against the relevant peptides has been demonstrated. In these cases, the high specificity is towards the free N-terminus of the peptidoglycan fragment. With a number of other enzymes, particularly high-molecular-mass DD-peptidases, little or no activity against these peptides was observed. In separate experiments, the reactivity of the enzymes against the central, largely invariant, peptide stem was examined. None of the enzymes surveyed showed high activity against this structural element although weak specificity in the expected direction towards the one structural variable (d-γGln versus d-γGlu) was observed. The current state of understanding of the activity of these enzymes in vitro is discussed.
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Sawada, Toshiki, Rina Oyama, Michihiro Tanaka, and Takeshi Serizawa. "Discovery of Surfactant-Like Peptides from a Phage-Displayed Peptide Library." Viruses 12, no. 12 (December 15, 2020): 1442. http://dx.doi.org/10.3390/v12121442.

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Peptides with specific affinities for various materials have been identified in the past three decades and utilized in materials science and engineering. A peptide’s capability to specifically interact with materials is not naturally derived but screened from a biologically constructed peptide library displayed on phages or cells. To date, due to limitations in the screening procedure, the function of screened peptides has been primarily limited to the affinity for target materials. Herein, we demonstrated the screening of surfactant-like peptides from a phage-displayed peptide library. A screened phage clone displaying a peptide showed high activity for accumulating at emulsion surfaces with certain assembled structures, resulting in stable emulsions. The surface tension for the solution of the chemically synthesized peptide decreased with increasing peptide concentration, demonstrating certain surface activity, which corresponded to the ability to decrease the surface tension of liquids (e.g., water), owing to the accumulation of molecules at the air–liquid or liquid–liquid interface. Peptides with a randomized sequence did not lower the surface tension, indicating the essential role of amino acid sequences in surface activity. Our strategy for identifying novel functional peptides from a phage-displayed peptide library can be used to expand the applicability of peptidyl materials and biosurfactants.
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Momburg, F., J. Roelse, G. J. Hämmerling, and J. J. Neefjes. "Peptide size selection by the major histocompatibility complex-encoded peptide transporter." Journal of Experimental Medicine 179, no. 5 (May 1, 1994): 1613–23. http://dx.doi.org/10.1084/jem.179.5.1613.

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The major histocompatibility complex (MHC)-encoded heterodimeric TAP1/TAP2 transporter (TAP) translocates cytosolic peptides into the lumen of the endoplasmic reticulum (ER), where peptides of 8 to 11 amino acids long associate with MHC class I molecules. We have studied the selectivity of peptide translocation by TAP in streptolysin O-permeabilized cells using glycosylatable, radioiodinated model peptides to detect import into the ER lumen. TAP-dependent translocation of a radiolabeled nonamer peptide was most efficiently inhibited by unlabeled 9- to 11-mer peptides. Peptides between 7 and 40 amino acids long all could inhibit transport, the longer peptides being least effective. Also, peptides shorter than eight amino acids were inefficiently translocated. The use of directly labeled length variants in translocation assays and TLC analysis of the transported material revealed two pathways for translocation: short peptides (7 to 13 amino acids long) were translocated without prior modification. In contrast, transport of longer peptides was not effective. Instead such peptides were clipped by cytosolic peptidases before efficient transport. Our data suggest that TAP preferentially translocates peptides of appropriate length for class I binding. Furthermore, TAP-translocated peptides were rapidly released from the ER unless they were trapped there by being glycosylated or by binding to MHC class I molecules.
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Ting, Yi Tian, Paul W. R. Harris, Gaelle Batot, Margaret A. Brimble, Edward N. Baker, and Paul G. Young. "Peptide binding to a bacterial signal peptidase visualized by peptide tethering and carrier-driven crystallization." IUCrJ 3, no. 1 (January 1, 2016): 10–19. http://dx.doi.org/10.1107/s2052252515019971.

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Bacterial type I signal peptidases (SPases) are membrane-anchored serine proteases that process the signal peptides of proteins exported via the Sec and Tat secretion systems. Despite their crucial importance for bacterial virulence and their attractiveness as drug targets, only one such enzyme, LepB from Escherichia coli, has been structurally characterized, and the transient nature of peptide binding has stymied attempts to directly visualize SPase–substrate complexes. Here, the crystal structure of SpsB, the type I signal peptidase from the Gram-positive pathogen Staphylococcus aureus, is reported, and a peptide-tethering strategy that exploits the use of carrier-driven crystallization is described. This enabled the determination of the crystal structures of three SpsB–peptide complexes, both with cleavable substrates and with an inhibitory peptide. SpsB–peptide interactions in these complexes are almost exclusively limited to the canonical signal-peptide motif Ala-X-Ala, for which clear specificity pockets are found. Minimal contacts are made outside this core, with the variable side chains of the peptides accommodated in shallow grooves or exposed faces. These results illustrate how high fidelity is retained despite broad sequence diversity, in a process that is vital for cell survival.
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Leszczyńska, Joanna, Agnieszka K. Szczepankowska, Iwona Majak, Dorota Mańkowska, Beata Smolińska, Sylwia Ścieszka, Anna Diowksz, Bożena Cukrowska, and Tamara Aleksandrzak-Piekarczyk. "Reducing Immunoreactivity of Gluten Peptides by Probiotic Lactic Acid Bacteria for Dietary Management of Gluten-Related Diseases." Nutrients 16, no. 7 (March 27, 2024): 976. http://dx.doi.org/10.3390/nu16070976.

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Immunoreactive gluten peptides that are not digested by peptidases produced by humans can trigger celiac disease, allergy and non-celiac gluten hypersensitivity. The aim of this study was to evaluate the ability of selected probiotic strains to hydrolyze immunoreactive gliadin peptides and to identify peptidase-encoding genes in the genomes of the most efficient strains. Residual gliadin immunoreactivity was measured after one- or two-step hydrolysis using commercial enzymes and bacterial peptidase preparations by G12 and R5 immunoenzymatic assays. Peptidase preparations from Lacticaseibacillus casei LC130, Lacticaseibacillus paracasei LPC100 and Streptococcus thermophilus ST250 strains significantly reduced the immunoreactivity of gliadin peptides, including 33-mer, and this effect was markedly higher when a mixture of these strains was used. In silico genome analyses of L. casei LC130 and L. paracasei LPC100 revealed the presence of genes encoding peptidases with the potential to hydrolyze bonds in proline-rich peptides. This suggests that L. casei LC130, L. paracasei LPC100 and S. thermophilus ST250, especially when used as a mixture, have the ability to hydrolyze immunoreactive gliadin peptides and could be administered to patients on a restricted gluten-free diet to help treat gluten-related diseases.
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Dissertations / Theses on the topic "Peptides"

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Zhang, Zhiwen. "Towards peptide-binding peptides." Access restricted to users with UT Austin EID, 2001. http://wwwlib.umi.com/cr/utexas/fullcit?p3037037.

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Howells, A. "Studies on peptides and peptide mimetics." Thesis, Swansea University, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.637318.

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Part 1: Development of a racemisation free process of attaching the first amino acid to a solid resin support for peptide synthesis. To overcome the high degree of racemisation of the amino acid in this process, we have explored a new kind of method of attaching this first amino acid to a resin. This approach involves activating the alcohol of the polyamide resin, instead of activating the amino acid. To test this theory we used benzyl alcohol as a model for the resin, and activated the alcohol with diisopropylcarbodiimide to form an O-isourea derivative. A detailed kinetic study was carried out to establish the rate of reaction with different benzyl alcohols, which proved that solution phase formation of the benzyl esters was successful. We were unable to attach the first amino acid to the resin support, which we believe is due to the reagents being unable to interact with the alcohol sites which are inside the bead of the resin. Part 2: Development of a novel peptidomimetic constraint. Current interest in the development of β-turn stabilising constraints for biologically active peptide motifs led us to synthesise a novel peptidomimetic molecule which in its cis form would provide a scaffold to constrain the conformation of a linear peptide. In stereochemically pure form the BocNH and CO2Et would be pointing in the right direction to mimic a β-bend, and could be a prototype for peptidomimetics based on e.g. cell adhesion and anti-aggregatory peptides. The synthesis proved demanding as this dioxopiperazine combines an α-diamino with a β-keto ester system, and although all linear precursors were satisfactorily synthesised, the final step which involved a cyclisation reaction did not work. To remove the complication of a β-keto ester system we then attempted to synthesise (36). (Fig. 3754) Again the pre-cyclisation stages were achieved satisfactorily to yield Z-NHCH(NHBoc)CONHCH(CH2OH)CO2CH3
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Chen, Fei. "Studies on aminoxy peptides and prebiotic peptide formation." Click to view the E-thesis via HKUTO, 2006. http://sunzi.lib.hku.hk/hkuto/record/B38534149.

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Chen, Fei, and 陳飛. "Studies on aminoxy peptides and prebiotic peptide formation." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2006. http://hub.hku.hk/bib/B38534149.

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Gudlur, Sushanth. "Peptide nanovesicles: supramolecular assembly of branched amphiphilic peptides." Diss., Kansas State University, 2012. http://hdl.handle.net/2097/13445.

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Doctor of Philosophy
Department of Biochemistry
John M. Tomich
Peptide-based delivery systems show great potential as safer drug delivery vehicles. They overcome problems associated with lipid-based or viral delivery systems, vis-a-vis stability, specificity, inflammation, antigenicity, and tune-ability. We have designed and synthesized a set of 15 and 23-residue branched, amphiphilic peptides that mimic phosphoglycerides in molecular architecture. They undergo supramolecular self-assembly and form solvent-filled, bilayer delineated spheres with 50-150 nm diameters (confirmed by TEM and DLS). Whereas weak hydrophobic forces drive and sustain lipid bilayer assemblies, these structures are further stabilized by β-sheet hydrogen bonding and are stable at very low concentrations and even in the presence of SDS, urea and trypsin as confirmed by circular dichroism spectroscopy. Given sufficient time, they fuse together to form larger assemblies and trap compounds of different sizes within the enclosed space. They are prepared using a protocol that is similar to preparing lipid vesicles. We have shown that different concentrations of the fluorescent dye, 5(6)-Carboxyfluorescein can be encapsulated in these assemblies and delivered into human lens epithelial cells and MCF-7 cells grown on coverslips. Besides fluorescent dyes, we have delivered the plasmid (EGFP-N3, 4.7kb) into N/N 1003A lens epithelial cells and observed expression of EGFP (in the presence and absence of a selection media). In the case of large molecules like DNA, these assemblies act as nanoparticles and offer some protection to DNA against certain nucleases. Linear peptides that lacked a branching point and other branched peptides with their sequences randomized did not show any of the lipid-like properties exhibited by the branched peptides. The peptides can be chemically decorated with target specific sequences for use as DDS for targeted delivery.
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Martari, Marco. "Structure-function relationships of bolaamphiphilic peptides and peptide hybrids." Thesis, Link to the online version, 2006. http://hdl.handle.net/10019/582.

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Charbonnier-Gérardin, Christine. "Nouvelles applications en synthèse des acides 2-dialkylphosphonoalcanoique : préparation de phosphonopeptides inhibiteurs de peptidases." Nancy 1, 1991. http://www.theses.fr/1991NAN10063.

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Une conception générale de synthèse de phosphonopeptides renfermant un motif phosphore du cote c-terminal ou du cote n-terminal est proposée à partir d'un même substrat acide 2-dialkylphosphonoalcanoique. L'objectif est de préparer des inhibiteurs de peptidases présentant une activité thérapeutique. L'approche la plus efficace pour introduire le motif phosphonate sous forme enantiomeriquement pure dans les phosphonopeptides n-terminaux consiste à utiliser la chaine peptidique chirale pour induire une asymétrie sur le carbone directement lié au phosphore. Le couplage peptidique a également été mis au point entre l'acide phosphonoacetique et l'acide 6-aminopenicillanique dans le but de préparer de nouveaux antibiotiques. L'étude du comportement des phosphonopeptides n-terminaux en tant que réactifs de Honer a été abordée pour préparer des peptides insaturés, substituts possibles de peptides à usage thérapeutique. Enfin, la réactivité de thiols sur les chlorures d'acides 2-dialkylphosphonoalcanoiques constitue une voie de synthèse de dialcoxyphosphorylalcane thioates de s-alkyle, qui conduisent eux-mêmes par réaction de Horner à des thioesters éthyléniques, cette réaction des généralisable aux dérivés chrysanthemiques
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Yiangou, Yiangos. "Studies on peptide-histidine isoleucine (PHI-27)-like peptides." Thesis, Imperial College London, 1988. http://hdl.handle.net/10044/1/47318.

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Puchelle, Valentin. "Peptide-polymer conjugates : divergent synthesis from the initiating peptides." Electronic Thesis or Diss., Sorbonne université, 2020. http://www.theses.fr/2020SORUS472.

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L’utilisation de peptides pour des applications biomédicales reste limitée, en raison de leur courte demi-vie biologique. Le greffage de polymères aux peptides a conduit à l’amélioration des propriétés du peptide. Les conjugués peptide-polymère peuvent être synthétisés par méthode convergente ou divergente. Alors que la première approche conduit à de faibles rendements, la deuxième est limitée à la polymérisation de monomères vinyliques. Nous proposons une méthode de synthèse divergente des conjugués, basée sur la fonctionnalisation des liaisons peptidiques, via le greffage de polyéthers. En effet, la polymérisation anionique par ouverture de cycle (AROP) des epoxides, à partir d’amorceurs amide, à été démontrée. Cette méthode polyvalente donne accès à des chaines de type PEG sans activation préalable. Les fonctions NH des amides de peptides ont été déprotonnées par une base phosphazène pour générer un amorceur de l’AROP. Des dipeptides cycliques (DKP) ont d’abord été utilisés pour démontrer la fonctionnalisation des fonctions NH. Des conditions de polymérisation ont été identifiées pour synthétiser de manière contrôlée des chaînes de polymères fonctionnalisées par une DKP. Le même système d’amorçage a été appliqué à un dipeptide, et des conjugués ont pu être synthétisés. Des essais ont été menés sur un tripeptide protégé et non protégé, mais se sont révélés peu concluants
Peptides as drugs are facing drawbacks such as short in-vivo half life and low resistance to enzymes, which limits a larger scale use. To overcome these shortcomings, conjugation of polymers to peptides leads to improvements of pharmacokinetic properties of the peptide. Peptide-polymers conjugates are synthesized either by convergent or divergent synthesis. While the first strategy faces low yields, the second one is limited to vinyl-based polymers. We aim to functionalize peptides on amide bonds by divergent synthesis of polyether from the peptide. Anionic Ring-Opening Polymerization (AROP) of epoxides has already proven to be feasible, from amide-based initiators. The approach is polyvalent and gives access to PEG-like polymers without activation of peptides prior synthesis. In this project, NH amide functions from small peptides were deprotonated by phosphazene base to generate an AROP initiator. First, cyclic dipeptides, were used to demonstrate the possible functionalization on NH functions. Polymerization conditions were identified for a controlled AROP, to afford polymers end-capped by a DKP. Initiator’s complexity was increased to protected linear dipeptide. Similar initiating system was used as previously, and conjugates could actually be synthesized. Initiating capacities of tri-peptides and protected tri-peptides were also investigated but were found to be inefficient
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Bagheri, Mojtaba [Verfasser]. "Cationic antimicrobial peptides : thermodynamic characterization of peptide-lipid interactions and biological efficacy of surface-tethered peptides / Mojtaba Bagheri." Berlin : Freie Universität Berlin, 2010. http://d-nb.info/1025126971/34.

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Books on the topic "Peptides"

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Tam, James P., and Pravin T. P. Kaumaya, eds. Peptides Frontiers of Peptide Science. Dordrecht: Springer Netherlands, 2002. http://dx.doi.org/10.1007/0-306-46862-x.

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Sāmī, Saʻīd, Mutt Viktor, and New York Academy of Sciences., eds. Vasoactive intestinal peptide and related peptides. New York, N.Y: New York Academy of Sciences, 1988.

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Wieland, Theodor. The world of peptides: A brief history of peptide chemistry. Berlin: Springer-Verlag, 1991.

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Boulton, Alan A., Glen B. Baker, and Q. J. Pittman. Peptides. New Jersey: Humana Press, 1987. http://dx.doi.org/10.1385/0896031055.

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Basava, Channa, and G. M. Anantharamaiah, eds. Peptides. Boston, MA: Birkhäuser Boston, 1994. http://dx.doi.org/10.1007/978-1-4615-8176-5.

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Smith, John A., and Jean E. Rivier, eds. Peptides. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1.

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Marshall, Garland R., ed. Peptides. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-010-9595-2.

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Hodges, Robert S., and John A. Smith, eds. Peptides. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0683-2.

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Rivier, Jean E., and Garland R. Marshall, eds. Peptides. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-010-9060-5.

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Du, Yu-cang, James P. Tam, and You-shang Zhang, eds. Peptides. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-010-9066-7.

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Book chapters on the topic "Peptides"

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Hruby, V. J. "Peptide chemistry:Designing peptides pseudopeptides and peptidomimetics for biological receptors." In Peptides, 3–17. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0683-2_1.

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Heath, Donald, and Paul Smith. "Peptides." In Diseases of the Human Carotid Body, 63–72. London: Springer London, 1992. http://dx.doi.org/10.1007/978-1-4471-1874-9_8.

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White, John Stephen, and Dorothy Chong White. "Peptides." In Proteins, Peptides and Amino Acids SourceBook, 207–669. Totowa, NJ: Humana Press, 2002. http://dx.doi.org/10.1007/978-1-59259-170-1_3.

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White, John Stephen, and Dorothy Chong White. "Peptides." In Proteins, Peptides and Amino Acids SourceBook, 671–713. Totowa, NJ: Humana Press, 2002. http://dx.doi.org/10.1007/978-1-59259-170-1_4.

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Seigler, David S. "Peptides." In Plant Secondary Metabolism, 234–46. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-4913-0_14.

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Ahluwalia, V. K., Lalita S. Kumar, and Sanjiv Kumar. "Peptides." In Chemistry of Natural Products, 67–111. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-86698-3_2.

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Avilés-Gaxiola, Sara, and J. Basilio Heredia. "Peptides." In Biological and Pharmacological Properties of the Genus Moringa, 113–26. New York: CRC Press, 2021. http://dx.doi.org/10.1201/9781003108863-7.

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Recio, Isidra, Lourdes Amigo, Blanca Hernández-Ledesma, and Beatriz Miralles. "Peptides." In Handbook of Dairy Foods Analysis, 33–64. 2nd ed. Second edition. | Boca Raton : CRC Press, 2021.: CRC Press, 2021. http://dx.doi.org/10.1201/9780429342967-4.

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Smith, Robert M., and Arthur E. Martell. "Peptides." In Critical Stability Constants, 128–58. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4615-6764-6_3.

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Kalidas, C., and M. V. Sangaranarayanan. "Peptides." In Biophysical Chemistry, 129–41. Cham: Springer Nature Switzerland, 2023. http://dx.doi.org/10.1007/978-3-031-37682-5_6.

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Conference papers on the topic "Peptides"

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REYMOND, JEAN-LOUIS. "PEPTIDE DENDRIMERS AND POLYCYCLIC PEPTIDES." In 23rd International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2014. http://dx.doi.org/10.1142/9789814603836_0003.

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Fresslnaud, E., J. E. Sadler, J. P. Girma, H. R. Baumgartner, and D. Meyer. "SYNTHETIC RGD-CONTAINING PEPTIDES OF VON WILLEBRAND FACTOR INHIBIT PLATELET ADHESION TO COLLAGEN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643591.

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The Arg-Gly-Asp (RGD) sequence is common to fibrinogen (Fg), fibronectin (Fn) and von Willebrand Factor (vWF). RGD-containing peptides compete for binding of these adhesive proteins to platelet membrane GPIIb/IIIa and inhibit thrombin-induced platelet aggregation as does an unrelated dodecapeptide from the γ Fg COOH terminus (γFg 400-411). We compared in flowing blood the effect of γ Fg 400-411 and of 3 synthetic peptides derived from the sequence of human vWF upon platelet adhesion to collagen. The 3 vWF peptides (13 or 18 aminoacids) contained an RGD sequence in the NH2 (peptide 03), central (peptide 07) or COOH (peptide 02) portions. Collagen was coated onto plastic coverslips and exposed in a parallel-plate perfusion chamber to reconstituted human blood at a shear rate of 2,600 s™1 for 3 min at 37°C. Perfusates contained physiological concentrations of 51 Cr-platelets and red cells in either citrated autologous plasma or modified Tyrode buffer containing 4% human albumin ; in the latter case, the collagen-coated coverslips were preincubated with normal plasma or purified human vWF prior to perfusion. Platelet-collagen interactions were estimated by radioactivity counting and quantitative morphometry. RGD peptides 02, 03 and 07 inhibited platelet-collagen interactions in a dose-dependent manner. With peptide 07, deposition of 51 Cr-platelets decreased from 283.8 ± 32.5 × 105/cm2 (mean ± SEM, n = 3) with buffer to 169.6 ± 33.0 in the presence of 50 μM peptide (p < 0.05), 133.7 ± 26.4 with 150 uM (p <0.012) and 101.8 ± 27.1 with 300 uM (p <0.005). The inhibitory effect of γ Fg 400-411 upon platelet deposition was less significant than that of the RGD peptides at 50 and 150 uM concentrations (224.4 ± 39.8, N.S. and 139.5 ± 55.3, p < 0.05, respectively). RGD peptide 07 also inhibited in a dose-dependent way both platelet adhesion to collagen and thrombus growth. Similar results were observed with peptides 02 and 03, indicating that the position of the RGD sequence is not critical. No synergetic effect between RGD and γFg 400-411 peptides was observed. These results with vWF peptides confirm that GPIIb/IIIa is involved not only In platelet aggregation (thrombus growth) but also in vWF-mediated platelet adhesion to collagen.
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Newton, Ashley, and Kaustav Majumder. "Evaluating the Efficacy of Germination in Producing Biologically Active Peptides from Garbanzo Beans." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/czkw6895.

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Interest in plant-based protein, specifically pulse protein, has grown exponentially. Garbanzo beans (Cicer arietinum) have gained interest, as they are commonly consumed in many parts of the world. Bioactive peptides identified in pulse proteins have been shown to increase in concentration when exposed to various processing methods. Germination has been shown to decrease antinutritional factor concentration and increase production of enzymes, resulting in the production of peptides with potential bioactivity. This experiment aims to evaluate the efficacy of germination in producing and increasing the concentration of bioactive peptides in garbanzo beans. Garbanzo beans (GB) were germinated over a 3-day time period, with samples taken at the start of germination (day 0) and day 3. Soluble protein content was analyzed by Lowry’s protein estimation method and peptide content was measured using a fluorometric peptide assay. SDS-PAGE gel electrophoresis was performed to investigate proteolytic changes in major storage proteins after germination. Soluble protein content and peptide content were both found to significantly increase after three days of germination. Germination of GB was found to increase the total soluble protein and peptide by 1% and 70%, respectively. Gel electrophoresis revealed the occurrence of proteolysis on day 3, with a disappearance of bands at 65 kDa and 100 kDa, corresponding to vicilin and convicilin, respectively, as well as a decrease in bands around 50 kDa, corresponding to legumin subunits. Future work will involve testing the bioactive potential of peptides derived from germinated GB using cell culture assays and identifying potential bioactive peptides via liquid chromatography-tandem mass spectrometry.Plant-based protein popularity has continued to increase, and there is a large interest in the use of bioactive peptides in pulses. The use of various processing conditions to increase the concentration of bioavailable peptides in pulses can be used to develop functional foods with novel health benefits.
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Liu, Dan-Xuan, Yi-Heng Xu, and Chao Qian. "Peptide Vaccine Design by Evolutionary Multi-Objective Optimization." In Thirty-Third International Joint Conference on Artificial Intelligence {IJCAI-24}. California: International Joint Conferences on Artificial Intelligence Organization, 2024. http://dx.doi.org/10.24963/ijcai.2024/770.

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Peptide vaccines are growing in significance for fighting diverse diseases. Machine learning has improved the identification of peptides that can trigger immune responses, and the main challenge of peptide vaccine design now lies in selecting an effective subset of peptides due to the allelic diversity among individuals. Previous works mainly formulated this task as a constrained optimization problem, aiming to maximize the expected number of peptide-Major Histocompatibility Complex (peptide-MHC) bindings across a broad range of populations by selecting a subset of diverse peptides with limited size; and employed a greedy algorithm, whose performance, however, may be limited due to the greedy nature. In this paper, we propose a new framework PVD-EMO based on Evolutionary Multi-objective Optimization, which reformulates Peptide Vaccine Design as a bi-objective optimization problem that maximizes the expected number of peptide-MHC bindings and minimizes the number of selected peptides simultaneously, and employs a Multi-Objective Evolutionary Algorithm (MOEA) to solve it. We also incorporate warm-start and repair strategies into MOEAs to improve efficiency and performance. We prove that the warm-start strategy ensures that PVD-EMO maintains the same worst-case approximation guarantee as the previous greedy algorithm, and meanwhile, the EMO framework can help avoid local optima. Experiments on a peptide vaccine design for COVID-19, caused by the SARS-CoV-2 virus, demonstrate the superiority of PVD-EMO.
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Stüber, W., H. Pelzer, and N. Heimburger. "INDUCTION OF ANTITHROMBIN III (AT III) ANTIBODIES BY IMMUNIZATION WITH SYNTHETIC PEPTIDES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644355.

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The primary structure of AT III was examined in respect of potential antigenic sites. The topics were the determination of the hydrophilicity, hydropathy, acrophilicity and the propensities for alpha-helices, B-turns and 13-sheets. The peptides AT III 21-34, 21-42, 129 - 140, 226 - 240 and 343 -363 were synthesized using the solid phase peptide synthesis methode. The subsequent purification of the crude peptides was achieved by h.p.I.e. or by ion exchange chromatography. The peptides were coupled to keyhole limpet hemocyanine (KLH) via thioether bonds. Antisera against KLH-peptides were raised in rabbits (n = 25) and tested with AT III-coated polystyrene tubes; bound antibodies were detected with anti-rabbit-IgG-peroxidase. Obtained antisera were further purified by immuno-adsorption using immobilized AT III. Polystyrene tubes were coated with purified peptide antibodies and binding of AT III was studied with enzyme immunoassay technique (EIA) using anti-AT III-peroxidase.As a result, immunoreactivity of rabbit antisera against synthetic peptides of AT III could be achieved. The obtained antibodies against the individual synthetic peptides as well as their mixtures exhibited specific binding to AT III when tested with EIA.
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Baba, Waqas, and Sajid Maqsood. "Novel antihypertensive and anticholesterolemic peptides from peptic hydrolysates of camel whey proteins." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/qecs2081.

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Hypercholesterolemia and hypertension are major growing concerns that are managed by drugs that inhibit various metabolic enzymes. Milk hydrolysates have been reported to contain various bioactive peptides (BAP) that can inhibit various metabolic enzymes for enhancing human health. As such camel whey proteins were subjected to peptic hydrolysis using a full factorial model (33) with hydrolysis time, temperature, and enzyme concentration as factors. The resulting hydrolysates were analyzed for anti-hypercholesterolemic and hypertensive properties by studying the in vitro inhibition of various enzymatic markers. The hydrolysates with lowest IC50 values were further subjected to LC-MS-QTOF that revealed presence of 185 peptides. Selected peptides that had Peptide Ranker Score greater than 0.8 were further studied for prediction of possible interactions with enzyme markers: pancreatic lipase (PL) cholesterol esterase (CE) and angiotensin converting enzyme (ACE) using in silico analysis. The data generated suggested that most of the peptides could bind active site of PL while as only three peptides could bind active site of CE. Based on higher number of reactive residues in the bioactive peptides (BAP) and greater number of substrate binding sites, FCCLGPVPP was identified as potential CE inhibitory peptide while PAGNFLPPVAAAPVM, MLPLMLPFTMGY, and LRFPL were identified as PL inhibitors. While peptides PAGNFLP, FCCLGPVPP, PAGNFLMNGLMHR, PAVACCLPPLPCHM were identified as potential ACE inhibitors. Molecular docking of selected peptides showed hydrophilic and hydrophobic interactions between peptides and target enzymes. Moreover, due to the importance of renin in managing hypertension, peptides from hydrolysates with high ACE inhibiting potential were predicted for potential to interact with renin using in silico analysis. Molecular docking was subsequently employed to identify how the identified peptides, PVAAAPVM and LRPFL, could interact with renin and potentially inhibit it. Thus, non-bovine (camel) whey hydrolysates might be used as functional ingredients for production of functional foods with antihypertensive and anticholesterolemic properties.
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D’Souza, S. E., M. H. Ginaberg, S. Lam, and E. A. Plow. "ACTIVATION DEPENDENT ALTERATIONS IN THE CHEMICAL CROSSLINKING OF ARGINYL-GLYCYL-ASPARTIC ACID (RGD) PEPTIDES WITH PLATELET GLYCOPROTEIN (GP) GPIIb-IIIa." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643699.

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The platelet adhesive proteins, fibrinogen, fibronectin and von WillebrandFactor, contain RGD amino acid sequences; RGD-containing peptides inhibit the binding of these adhesive proteins to platelets; and a membrane receptor for these adhesive proteins binds to Arg-Gly-Asp and contains GPIIb-IIIa. The present study was undertaken to characterize the interaction of RGDpeptides with GPIIb-IIIa using a chemical crosslinking approach. A radioiodinated RGD-containing heptapeptide was bound to washed human platelets under conditions at which ≥ 85% of theinteraction was inhibited by excess nonlabeled peptide. After binding of the peptide to platelets for 45 min at22°, a homobifunctional crosslinking reagent was added, and the platelets were extracted and analyzed on polyacrylamide gels. With resting platelets,autoradiography of the gels revealedthat the peptide crosslinked tobothGPIIb and GPIIIa. This interaction wasinhibited by excess nonlabeled peptide but not by certain conservatively substituted RGD peptides. Stimulation of the platelets caused a dramatic increase in crosslinking of the peptide to only one of the two subunitsof GPIIb-IIIa. The stimulus dependentincrease in the crosslinking reactionwas specific and saturable as it was inhibited by RGD peptides in a dose dependent manner. In addition, peptides corresponding in structure to the carboxy terminus of the γ chain of fibrinogen also produced concentration dependent inhibition of the interaction. The increase in crosslinking induced by platelet stimulation was divalent ion dependent. Similar results werealso obtained with a second, larger RGD-containing peptide and with asecond chemical crosslinking reagent.Theseresults indicate that platelet stimulation in the presence of divalent ions causes a change which permitsmoreefficient crosslinking of RGD-containing peptides to only one of the two subunits of GPIIb-IIIa. The results are also compatible with a proximalrelationship of both subunits tothe RGD binding sites on the plateletmembrane.
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Westwood, Brian M., Hossam A. Shaltout, and Mark C. Chappell. "Modeling of Angiotensin Peptide Metabolism in Renal Proximal Tubules." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-190990.

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The recent discovery of angiotensin converting enzyme 2 (ACE2) as a functional peptidase within the renin-angiotensin system (RAS) has added a new layer of complexity to the enzymatic cascade of this hormonal system. ACE2 is highly expressed in the proximal tubules of the kidney, an important tissue site involved in blood pressure regulation. Therefore, we derived a model for the processing of Ang I which is the immediate precursor to the biologically active peptides Ang II and Ang-(1-7) based on metabolism data in isolated proximal tubules of the sheep kidney (1). Given the individual experimental velocities for several peptidases expressed in the proximal tubules including ACE, ACE2 and neprilysin, rate constants were calculated to describe the conservation equations for the processing of Ang I, Ang II and Ang-(1-7) We modeled the system with Ang I as the initial substrate and peptide concentrations for the downstream products were calculated using Euler’s method.
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Fulcher, C. A., R. A. Houghten, S. de Graaf Mahoney, J. R. Roberts, and T. S. Zimmerman. "SYNTHETIC PEPTIDE PROBES OF FACTOR VIII IMMUNOLOGY AND FUNCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644768.

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In order to develop specific immunologic reagents for mapping functionally important sites on FVIII, we have prepared rabbit polyclonal antibodies against synthetic peptides of FVIII derived from regions along the entire FVIII amino acid sequence. To date, a total of 70 peptides have been synthesized and characterized by amino acid and HPLC analysis. The peptides were coupled to keyhole limpet hemocyanin with glutaraldehyde as a linkage reagent and used to immunize rabbits. Antisera were tested by ELISA assay on polystyrene microtiter plates coated with either the peptide immunogen, or purified FVIII. The antisera were also tested for their ability to inhibit FVIII clotting activity and to react with separated FVIII polypeptides on immunoblots.Of the 70 peptides, all reacted with the peptide immunogen, 45 reacted with purified FVIII and 33 reacted with FVIII on immunoblots. Because we had obtained evidence that cleavage of the amino terminal region of the 80 kDa polypeptide may play a role in FVIII activation by thrombin, a series of partially overlapping peptides, 15 residues in length, were synthesized in this area. After affinity purifying these antibodies on columns of FVIII immobilized on agarose, adjusting the antibodies to equal antigen binding titers by dot immunoblotting and testing for inhibition of FVIII activity, only one antibody could strongly inhibit FVIII clotting activity. This inhibition could be blocked by the peptide itself at nanomolar concentrations and no significant inhibition could be shown by antibodies to partially overlapping peptides individually, or in combination. These data suggest that a site important to FVIII function can be localized to a 15 amino acid residue region of the 80 kDa polypeptide of FVIII. In addition, a second inhibitoryantibody was identified which was produced against a peptide in the carboxy terminal region of the 54 kDa thrombin fragment of FVIII and this area is currently being studied in a similar manner. In addition, two monoclonal anti-FVIII synthetic peptide antibodies have been produced which react with purified FVIII on immunoblots. One of these antibodies also functions as an immunoadsorbent when linked to agarose and FVII can be purified in this manner, using the synthetic peptide as eluant. It is evident that antibodies to synthetic peptides of FVIII can be useful probes of FVIII structure, function and interactions as well as being of use in FVIII purification.
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Bjørlie, Mads, Rachel Irankunda, Jean-Michel Girardet, Sandrine Boschi-Müller, Betül Yesiltas, Charlotte Jacobsen, and Laetitia Canabady-Rochelle. "Screening of Metal-chelating Peptides and Hydrolysates Using Surface Plasmon Resonance and Switchsense." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/zszk2778.

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Abstract: Lipid oxidation is, among other factors, catalyzed by the presence of metal ions and efficient metal chelators are therefore highly sought after in the food industry. Among these, natural metal chelators are gaining interest as opposed to their synthetic counterparts such as EDTA. Traditional screening for metal chelation capacity is time consuming and non-specific. The aim of this study was to screen potato protein hydrolysate and synthetic peptides derived from potato protein sequences for their metal-chelating capacity. Seven peptides and two hydrolysates (raw and ultra-filtrated) were studied. Peptides were selected using two different models: an empirical-based bioinformatics approach (AnOxPePred) and a theoretically based model for metal chelation. Surface Plasmon Resonance (SPR) is a label-free, optical technique used to determine the dissociation constant (KD) of a complex formed between immobilized Ni2+ and peptides. The SwitchSENSE technology is another approach used to study Ni2+/peptide affinity. It utilizes the quenching of fluorescence of a fluorophore upon Ni2+ immobilization and the inverse fluorescence increase upon peptide binding onto Ni2+. Both analyses were carried out at pH 7.4. In this study, we successfully determined the dissociation constants (KD) of two peptides (ASH and DHGPKIFEPS) using SPR. These values compare favourably with previous results indicating metal chelating potential. The association rate constant (kon) of all peptides were determined using switchSENSE. Yet, due to bad fitting of the kinetics data obtained with switchSENSE, the KDs of the hydrolysates were only determined with low accuracy.
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Reports on the topic "Peptides"

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Vouros, Paul, and Terrance Black. Solid Phase Peptide Synthesis of Antimicrobial Peptides for cell Binding Studies: Characterization Using Mass Spectrometry. Fort Belvoir, VA: Defense Technical Information Center, November 2002. http://dx.doi.org/10.21236/ada412571.

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Sharma, M. M., and G. Georgiou. Microbial enhanced oil recovery research. [Peptides]. Office of Scientific and Technical Information (OSTI), January 1992. http://dx.doi.org/10.2172/7053191.

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Sharma, M. M., and G. Georgiou. Microbial enhanced oil recovery research. [Peptides]. Office of Scientific and Technical Information (OSTI), January 1991. http://dx.doi.org/10.2172/6878180.

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Porkka, Kimmo. Tumor Targeting Peptides for Cytotoxic Chemotherapy. Fort Belvoir, VA: Defense Technical Information Center, July 2000. http://dx.doi.org/10.21236/ada391964.

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Wong, Eric A., and Zehava Uni. Nutrition of the Developing Chick Embryo: Nutrient Uptake Systems of the Yolk Sac Membrane and Embryonic Intestine. United States Department of Agriculture, June 2012. http://dx.doi.org/10.32747/2012.7697119.bard.

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We have examined the developmental changes in composition, amount, and uptake of yolk nutrients (fat, protein, water and carbohydrates) and the expression ofnutrient transporters in the yolk sac membrane (YSM) from embryonic day 11 (Ell) to 21 (E21) and small intestine from embryonic day 15 (E15) to E21 in embryos from young (22-25 wk) and old (45-50 wk) Cobb and Leghorn breeder flocks. The developmental expression profiles for the peptide transporter 1 (PepTl), the amino acid transporters, EAAT3, CAT-1 and BOAT, the sodium glucose transporter (SGLTl), the fructose transporter (GLUT5), the digestive enzymes aminopeptidase N (APN) and sucraseisomaltase (SI) were assayed by the absolute quantification real time PCR method in the YSM and embryonic intestine. Different temporal patterns of expression were observed for these genes. The effect of in ovo injection of peptides (the dipeptide Gly-Sar, purified peptides, trypsin hydrolysate) on transporter gene expression has been examined in the embryonic intestine. Injection of a partial protein hydrolysate resulted in an increase in expression of the peptide transporter PepT2. We have initiated a transcriptome analysis of genes expressed in the YSM at different developmental ages to better understand the function of the YSM.
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Horwitz, Benjamin, and Barbara Gillian Turgeon. Secondary Metabolites, Stress, and Signaling: Roles and Regulation of Peptides Produced by Non-ribosomal Peptide Synthetases. United States Department of Agriculture, 2005. http://dx.doi.org/10.32747/2005.7696522.bard.

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Fungal pathogens of plants produce a diverse array of small molecules. Often referred to as secondary metabolites because they were thought to be dispensable for basic functions, they may indeed have central roles as signals for the fungal cell, and in interactions with the host. We have identified more than a dozen genes encoding nonribosomal peptide synthetases (NPS) in Cochliobolusheterostrophus, the agent of southern corn leaf blight. The aim of this project was to identify roles of these genes in stress responses and signaling. The first objective was to test a complete collection of C. heterostrophus nonribosomal peptide synthetase (NRPS)-encoding gene deletion mutant and wildtype (WT) strains for sensitivity to various agents of oxidative (ROS) and nitrosative (RNOS) stress, in vitro. The second objective and next step in this part of the project was to study the relevance of sensitivity to ROS and RNOS in the host pathogen interaction, by measuring the production of ROS and RNOS in planta, when plants are inoculated with wild type and mutant strains. A third objective was to study expression of any genes shown to be involved in sensitivity to ROS or RNOS, in vitro and in planta. Another objective was to determine if any of the genes involved in oxidative or nitrosative stress responses are regulated by components of signal transduction pathways (STP) that we have identified and to determine where mechanisms overlap. Study of the collection of nps mutants identified phenotypes relevant for virulence, development and oxidative stress resistance for two of the genes, NPS2 and NPS6. Mutants in genes related to RNOS stress have no virulence phenotypes, while some of those related to ROS stress have reduced virulence as well as developmental phenotypes, so we focused primarily on ROS stress pathways. Furthermore, the identification of NPS2 and NPS6 as encoding for NRPS responsible for siderophore biosynthesis lent a new focus to the project, regulation by Fe. We have not yet developed good methods to image ROS in planta and work in this direction is continuing. We found that NPS6 expression is repressed by Fe, responding over the physiological Fe concentration range. Studying our collection of mutants, we found that conserved MAPK and G protein signal transduction pathways are dispensable for Fe regulation of NPS6, and initiated work to identify other pathways. The transcription factor SreA is one candidate, and is responsible for part, but not all, of the control of NPS6 expression. The results of this project show that the pathogen contends with oxidative stress through several signaling pathways. Loss of the siderophore produced by Nps6 makes the fungus sensitive to oxidative stress, and decreases virulence, suggesting a central role of the ability to sequester and take up extracellular iron in the host-pathogen interaction. Siderophores, and manipulation of Fe levels, could be targets for new strategies to deal with fungal pathogens of maize and other plants.
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Tiwari, Raj K. Tumor Associated Antigenic Peptides in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, March 2002. http://dx.doi.org/10.21236/ada406458.

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Wickstrom, Eric. Oncogene mRNA Imaging with Radionuclide-PNA-Peptides. Office of Scientific and Technical Information (OSTI), March 2008. http://dx.doi.org/10.2172/925560.

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Porkka, Kimmo. Tumor Targeting Peptides for Cytotoxic Chemotherapy Delivery. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada411410.

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Zhu, Chao-Zhi, Joseph G. Sebranek, and Dong U. Ahn. Antioxidant Peptides in Commercial Dry-Cured Hams. Ames (Iowa): Iowa State University, January 2016. http://dx.doi.org/10.31274/ans_air-180814-1388.

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