Relevant bibliographies by topics / Short-peptide Derivative

Academic literature on the topic 'Short-peptide Derivative'

Author: Grafiati
Published: 7 September 2023

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Journal articles on the topic "Short-peptide Derivative"

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Sugiura, Takumi, Takurou Kanada, Daisuke Mori, Hiroyuki Sakai, Aya Shibata, Yoshiaki Kitamura, and Masato Ikeda. "Chemical stimulus-responsive supramolecular hydrogel formation and shrinkage of a hydrazone-containing short peptide derivative." Soft Matter 16, no. 4 (2020): 899–906. http://dx.doi.org/10.1039/c9sm01969c.

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Mei, Jingjing, Xiaoli Zhang, Meifeng Zhu, Jianing Wang, Ling Wang, and Lianyong Wang. "Barium-triggered β-sheet formation and hydrogelation of a short peptide derivative." RSC Adv. 4, no. 3 (2014): 1193–96. http://dx.doi.org/10.1039/c3ra45023f.

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Belyaeva, Veronika S., Yulia V. Stepenko, Igor I. Lyubimov, Alexandr L. Kulikov, Alesia A. Tietze, Indira S. Kochkarova, Olga V. Martynova, et al. "Non-hematopoietic erythropoietin-derived peptides for atheroprotection and treatment of cardiovascular diseases." Research Results in Pharmacology 6, no. 3 (September 30, 2020): 75–86. http://dx.doi.org/10.3897/rrpharmacology.6.58891.

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Relevance: Cardiovascular diseases continue to be the leading cause of premature adult death. Lipid profile and atherogenesis: Dislipidaemia leads to subsequent lipid accumulation and migration of immunocompetent cells into the vessel intima. Macrophages accumulate cholesterol forming foam cells – the morphological substrate of atherosclerosis in its initial stage. Inflammation and atherogenesis: Pro-inflammatory factors provoke oxidative stress, vascular wall damage and foam cells formation. Endothelial and mitochondrial dysfunction in the development of atherosclerosis: Endothelial mitochondria are some of the organelles most sensitive to oxidative stress. Damaged mitochondria produce excess superoxide and H2O2, which are the main factors of intracellular damage, further increasing endothelial dysfunction. Short non-hematopoietic erythropoietin-based peptides as innovative atheroprotectors: Research in recent decades has shown that erythropoietin has a high cytoprotective activity, which is mainly associated with exposure to the mitochondrial link and has been confirmed in various experimental models. There is also a short-chain derivative, the 11-amino acid pyroglutamate helix B surface peptide (PHBSP), which selectively binds to the erythropoietin heterodymic receptor and reproduces its cytoprotective properties. This indicates the promising use of short-chain derivatives of erythropoietin for the treatment and prevention of atherosclerotic vascular injury. In the future, it is planned to study the PHBSP derivatives, the modification of which consists in adding RGD and PGP tripeptides with antiaggregant properties to the original 11-member peptide.
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Radzishevsky, Inna S., Shahar Rotem, Fadia Zaknoon, Leonid Gaidukov, Arie Dagan, and Amram Mor. "Effects of Acyl versus Aminoacyl Conjugation on the Properties of Antimicrobial Peptides." Antimicrobial Agents and Chemotherapy 49, no. 6 (June 2005): 2412–20. http://dx.doi.org/10.1128/aac.49.6.2412-2420.2005.

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ABSTRACT To investigate the importance of increased hydrophobicity at the amino end of antimicrobial peptides, a dermaseptin derivative was used as a template for a systematic acylation study. Through a gradual increase of the acyl moiety chain length, hydrophobicity was monitored and further modulated by acyl conversion to aminoacyl. The chain lengths of the acyl derivatives correlated with a gradual increase in the peptide's global hydrophobicity and stabilization of its helical structure. The effect on cytolytic properties, however, fluctuated for different cells. Whereas acylation gradually enhanced hemolysis of human red blood cells and antiprotozoan activity against Leishmania major, bacteria displayed a more complex behavior. The gram-positive organism Staphylococcus aureus was most sensitive to intermediate acyl chains, while longer acyls gradually led to a total loss of activity. All acyl derivatives were detrimental to activity against Escherichia coli, namely, but not solely, because of peptide aggregation. Although aminoacyl derivatives behaved essentially similarly to the nonaminated acyls, they displayed reduced hydrophobicity, and consequently, the long-chain acyls enhanced activity against all microorganisms (e.g., by up to 12-fold for the aminolauryl derivative) but were significantly less hemolytic than their acyl counterparts. Acylation also enhanced bactericidal kinetics and peptide resistance to plasma proteases. The similarities and differences upon acylation of MSI-78 and LL37 are presented and discussed. Overall, the data suggest an approach that can be used to enhance the potencies of acylated short antimicrobial peptides by preventing hydrophobic interactions that lead to self-assembly in solution and, thus, to inefficacy against cell wall-containing target cells.
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Giannecchini, Simone, Armida Di Fenza, Anna Maria D'Ursi, Donatella Matteucci, Paolo Rovero, and Mauro Bendinelli. "Antiviral Activity and Conformational Features of an Octapeptide Derived from the Membrane-Proximal Ectodomain of the Feline Immunodeficiency Virus Transmembrane Glycoprotein." Journal of Virology 77, no. 6 (March 15, 2003): 3724–33. http://dx.doi.org/10.1128/jvi.77.6.3724-3733.2003.

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ABSTRACT Feline immunodeficiency virus (FIV) provides a valuable animal model by which criteria for lentivirus control strategies can be tested. Previous studies have shown that a 20-mer synthetic peptide of the membrane-proximal ectodomain of FIV transmembrane glycoprotein, designated peptide 59, potently inhibited the growth of tissue culture-adapted FIV in feline fibroblastoid CrFK cells. In the present report we describe the potential of this peptide to inhibit the replication of primary FIV isolates in lymphoid cells. Because antiviral activity of peptide 59 was found to map to a short segment containing three conserved Trp residues, further analyses focused on a derivative of eight amino acids (770W-I777), designated C8. Peptide C8 activity was found to be dependent on conservation of the Trp motif, to be removed from solution by FIV absorbed onto substrate cells, and to be blocked by a peptide derived from the N-terminal portion of FIV transmembrane glycoprotein. Structural studies showed that peptide C8 possesses a conformational propensity highly uncommon for peptides of its size, which may account for its considerable antiviral potency in spite of small size.
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Bai, Fengwei, Terrence Town, Deepti Pradhan, Jonathan Cox, Ashish, Michel Ledizet, John F. Anderson, et al. "Antiviral Peptides Targeting the West Nile Virus Envelope Protein." Journal of Virology 81, no. 4 (December 6, 2006): 2047–55. http://dx.doi.org/10.1128/jvi.01840-06.

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ABSTRACT West Nile virus (WNV) can cause fatal murine and human encephalitis. The viral envelope protein interacts with host cells. A murine brain cDNA phage display library was therefore probed with WNV envelope protein, resulting in the identification of several adherent peptides. Of these, peptide 1 prevented WNV infection in vitro with a 50% inhibition concentration of 67 μM and also inhibited infection of a related flavivirus, dengue virus. Peptide 9, a derivative of peptide 1, was a particularly potent inhibitor of WNV in vitro, with a 50% inhibition concentration of 2.6 μM. Moreover, mice challenged with WNV that had been incubated with peptide 9 had reduced viremia and fatality compared with control animals. Peptide 9 penetrated the murine blood-brain barrier and was found in the brain parenchyma, implying that it may have antiviral activity in the central nervous system. These short peptides serve as the basis for developing new therapeutics for West Nile encephalitis and, potentially, other flaviviruses.
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Falla, T. J., and R. E. Hancock. "Improved activity of a synthetic indolicidin analog." Antimicrobial Agents and Chemotherapy 41, no. 4 (April 1997): 771–75. http://dx.doi.org/10.1128/aac.41.4.771.

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A novel cationic peptide, CP-11, based on the structure of the bovine neutrophil peptide indolicidin, was designed to increase the number of positively charged residues, maintain the short length (13 amino acids), and enhance the amphipathicity relative to those of indolicidin. CP-11, and especially its carboxymethylated derivative, CP-11C, demonstrated improved activity against gram-negative bacteria and Candida albicans, while it maintained the activity of indolicidin against staphylococci and demonstrated a reduced ability to lyse erythrocytes. In Escherichia coli, CP-11 was better able than indolicidin to permeabilize both the outer membrane, as indicated by the enhancement of uptake of 1-N-phenylnaphthylamine, and the inner membrane, as determined by the unmasking of cytoplasmic beta-galactosidase, providing an explanation for its improved activity.
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Praveen, Praveen, Chao Wang, Thomas N. G. Handley, Hongkang Wu, Chrishan S. Samuel, Ross A. D. Bathgate, and Mohammed Akhter Hossain. "A Lipidated Single-B-Chain Derivative of Relaxin Exhibits Improved In Vitro Serum Stability without Altering Activity." International Journal of Molecular Sciences 24, no. 7 (April 1, 2023): 6616. http://dx.doi.org/10.3390/ijms24076616.

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Human relaxin-2 (H2 relaxin) is therapeutically very important due to its strong anti-fibrotic, vasodilatory, and cardioprotective effects. Therefore, relaxin’s receptor, relaxin family peptide receptor 1 (RXFP1), is a potential target for the treatment of fibrosis and related disorders, including heart failure. H2 relaxin has a complex two-chain structure (A and B) and three disulfide bridges. Our laboratory has recently developed B7-33 peptide, a single-chain agonist based on the B-chain of H2 relaxin. However, the peptide B7-33 has a short circulation time in vitro in serum (t1/2 = ~6 min). In this study, we report structure-activity relationship studies on B7-33 utilizing different fatty-acid conjugations at different positions. We have shown that by fatty-acid conjugation with an appropriate spacer length, the in vitro half-life of B7-33 can be increased from 6 min to 60 min. In the future, the lead lipidated molecule will be studied in animal models to measure its PK/PD properties, which will lead to their pre-clinical applications.
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Rosa, Elisabetta, Enrico Gallo, Teresa Sibillano, Cinzia Giannini, Serena Rizzuti, Eliana Gianolio, Pasqualina Liana Scognamiglio, Giancarlo Morelli, Antonella Accardo, and Carlo Diaferia. "Incorporation of PEG Diacrylates (PEGDA) Generates Hybrid Fmoc-FF Hydrogel Matrices." Gels 8, no. 12 (December 16, 2022): 831. http://dx.doi.org/10.3390/gels8120831.

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Generated by a hierarchical and multiscale self-assembling phenomenon, peptide-based hydrogels (HGs) are soft materials useful for a variety of applications. Short and ultra-short peptides are intriguing building blocks for hydrogel fabrication. These matrices can also be obtained by mixing low-molecular-weight peptides with other chemical entities (e.g., polymers, other peptides). The combination of two or more constituents opens the door to the development of hybrid systems with tunable mechanical properties and unexpected biofunctionalities or morphologies. For this scope, the formulation, the multiscale analysis, and the supramolecular characterization of novel hybrid peptide-polymer hydrogels are herein described. The proposed matrices contain the Fmoc-FF (Nα-fluorenylmethyloxycarbonyl diphenylalanine) hydrogelator at a concentration of 0.5 wt% (5.0 mg/mL) and a diacrylate α-/ω-substituted polyethylene-glycol derivative (PEGDA). Two PEGDA derivatives, PEGDA 1 and PEGDA2 (mean molecular weights of 575 and 250 Da, respectively), are mixed with Fmoc-FF at different ratios (Fmoc-FF/PEGDA at 1/1, 1/2, 1/5, 1/10 mol/mol). All the multicomponent hybrid peptide-polymer hydrogels are scrutinized with a large panel of analytical techniques (including proton relaxometry, FTIR, WAXS, rheometry, and scanning electronic microscopy). The matrices were found to be able to generate mechanical responses in the 2–8 kPa range, producing a panel of tunable materials with the same chemical composition. The release of a model drug (Naphthol Yellow S) is reported too. The tunable features, the different topologies, and the versatility of the proposed materials open the door to the development of tools for different applicative areas, including diagnostics, liquid biopsies and responsive materials. The incorporation of a diacrylate function also suggests the possible development of interpenetrating networks upon cross-linking reactions. All the collected data allow a mutual comparison between the different matrices, thus confirming the significance of the hybrid peptide/polymer-based methodology as a strategy for the design of innovative materials.
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Barreto-Santamaría, Adriana, Zuly Jenny Rivera, Javier Eduardo García, Hernando Curtidor, Manuel Elkin Patarroyo, Manuel Alfonso Patarroyo, and Gabriela Arévalo-Pinzón. "Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance." Microorganisms 8, no. 6 (June 8, 2020): 867. http://dx.doi.org/10.3390/microorganisms8060867.

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Antimicrobial peptides (AMPs) have been recognised as a significant therapeutic option for mitigating resistant microbial infections. It has been found recently that Plasmodium falciparum-derived, 20 residue long, peptide 35409 had antibacterial and haemolytic activity, making it an AMP having reduced selectivity, and suggesting that it should be studied more extensively for obtaining new AMPs having activity solely targeting the bacterial membrane. Peptide 35409 was thus used as template for producing short synthetic peptides (<20 residues long) and evaluating their biological activity and relevant physicochemical characteristics for therapeutic use. Four of the sixteen short peptides evaluated here had activity against E. coli without any associated haemolytic effects. The 35409-1 derivative (17 residues long) had the best therapeutic characteristics as it had high selectivity for bacterial cells, stability in the presence of human sera, activity against E. coli multiresistant clinical isolates and was shorter than the original sequence. It had a powerful membranolytic effect and low potential for inducing resistance in bacteria. This peptide’s characteristics highlighted its potential as an alternative for combating infection caused by E. coli multiresistant bacteria and/or for designing new AMPs.
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Dissertations / Theses on the topic "Short-peptide Derivative"

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Lin, Tao. "Self-Assembly of Short Peptide Derivatives." The Ohio State University, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=osu161012283431265.

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Conte, Maria Paola. "Directing the self-assembly of short peptide derivatives." Thesis, University of Strathclyde, 2017. http://digitool.lib.strath.ac.uk:80/R/?func=dbin-jump-full&object_id=28511.

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Self-assembly of molecular building blocks has attracted increasing interest as an effective bottom-up approach for the design of functional nanomaterials. Amongst the variety of known molecular building blocks, very short (di- and tri-) peptides and their derivatives are of particular relevance in this context due to their chemical simplicity, low cost and remarkable properties. In this thesis, we first investigate the behaviour of the well-known self-assembling dipeptide diphenylalanine (FF) and its amidated derivative (FF-NH2) in a predominantly aqueous environment. We demonstrate that these molecules can form metastable hydrogels upon a combination of solvent switching and sonication of the dipeptide solutions. The hydrogels show instantaneous syneresis upon mechanical contact resulting in rapid expulsion of water and collapse into a semi-solid gel. Thanks to the highlyhydrophobic nature of the fibres formed, the gels can be employed as selective scavengers for small hydrophobic molecules. Combining biocatalysis and molecular self-assembly provides an effective approach for processing of self-assembled materials, directing the assembly kinetics by means of catalysis which results in the controlled formation of hierarchical nanostructures. Herein, we investigate the possibility to achieve localised self-assembly of peptide derivatives exploiting different strategies to immobilize enzymes, thereby adding spatial control over the self-assembly process. We functionalised surfaces with bioinspired polydopamine and polyphenol coatings to study the effects of enzyme surface localisation and surface release on the self-assembly process. We demonstrate how these coatings could be conveniently used to release protease enzyme thermolysin into a pre-gelator (Fmoc-T and F-NH2) solution for bulk gelation as well as to irreversibly immobilize the enzyme for localizing the self-assembly to the surface. Enzyme-(magnetic)nanoparticle conjugates were employed to trigger the self-assembly and gelation of peptide derivatives in two different systems, an equilibrium system and a far from equilibrium one. For both systems, the self-assembly results in the formation of stable hydrogels. We were able to visualise the self-assembled nanostructures at the site of enzyme immobilization by electron microscopy. Moreover, employing magnetic nanoparticles allows for an additional level of control on the properties of the hydrogels, which can be manipulated with an external magnetic field. Finally, we employed a soft-lithographic technique (microcontact printing) to transfer a pattern of enzymes onto a modified substrate. The surfaces with the patterned thermolysin were used to trigger the localized formation of the gelator Fmoc-TF-NH2 through direct condensation of two non-assembling precursors Fmoc-T and F-NH2. Fluorescence microscopy was employed to confirm the localized formation of self-assembled structure by staining the β-sheet fibres with Thioflavin T. The thesis concludes with a number of overall conclusions that can be drawn from the work presented, as well as some possible directions for future work.
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