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Journal articles on the topic 'Peptides antimicrobien'

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Published: 4 June 2021

Last updated: 16 February 2022

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1

Hwang, Peter M., and Hans J. Vogel. "Structure-function relationships of antimicrobial peptides." Biochemistry and Cell Biology 76, no. 2-3 (1998): 235–46. http://dx.doi.org/10.1139/o98-026.

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Antimicrobial peptides are ubiquitously produced throughout nature. Many of these relatively short peptides (6-50 residues) are lethal towards bacteria and fungi, yet they display minimal toxicity towards mammalian cells. All of the peptides are highly cationic and hydrophobic. It is widely believed that they act through nonspecific binding to biological membranes, even though the exact nature of these interactions is presently unclear. High-resolution nuclear magnetic resonance (NMR) has contributed greatly to knowledge in this field, providing insight about peptide structure in aqueous solut

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Bechinger, B., and S. U. Gorr. "Antimicrobial Peptides: Mechanisms of Action and Resistance." Journal of Dental Research 96, no. 3 (2016): 254–60. http://dx.doi.org/10.1177/0022034516679973.

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More than 40 antimicrobial peptides and proteins (AMPs) are expressed in the oral cavity. These AMPs have been organized into 6 functional groups, 1 of which, cationic AMPs, has received extensive attention in recent years for their promise as potential antibiotics. The goal of this review is to describe recent advances in our understanding of the diverse mechanisms of action of cationic AMPs and the bacterial resistance against these peptides. The recently developed peptide GL13K is used as an example to illustrate many of the discussed concepts. Cationic AMPs typically exhibit an amphipathic

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Gasu, Edward Ntim, Hubert Senanu Ahor, and Lawrence Sheringham Borquaye. "Peptide Extract from Olivancillaria hiatula Exhibits Broad-Spectrum Antibacterial Activity." BioMed Research International 2018 (December 23, 2018): 1–11. http://dx.doi.org/10.1155/2018/6010572.

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Increasing reports of infectious diseases worldwide have become a global concern in recent times. Depleted antibiotic pipelines, rapid and complex cases of antimicrobial resistance, and emergence and re-emergence of infectious disease have necessitated an urgent need for the development of new antimicrobial therapeutics, preferably with novel modes of action. Due to their distinct mode of action, antimicrobial peptides offer an interesting alternative to conventional antibiotics to deal with the problems enumerated. In this study, the antimicrobial potential of the peptide extract from the mar

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Bachrach, Gilad, Hamutal Altman, Paul E. Kolenbrander, et al. "Resistance of Porphyromonas gingivalis ATCC 33277 to Direct Killing by Antimicrobial Peptides Is Protease Independent." Antimicrobial Agents and Chemotherapy 52, no. 2 (2007): 638–42. http://dx.doi.org/10.1128/aac.01271-07.

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ABSTRACT Antimicrobial peptides are short, positively charged, amphipathic peptides that possess a wide spectrum of antimicrobial activity and have an important role in the host's innate immunity. Lack of, or dysfunctions in, antimicrobial peptides have been correlated with infectious diseases, including periodontitis. Porphyromonas gingivalis, a gram-negative anaerobe and a major pathogen associated with periodontal diseases, is resistant to antimicrobial peptides of human and nonhuman origin, a feature that likely contributes to its virulence. Expressing a robust proteolytic activity, P. gin

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López-García, Belén, Luis González-Candelas, Enrique Pérez-Payá, and Jose F. Marcos. "Identification and Characterization of a Hexapeptide with Activity Against Phytopathogenic Fungi That Cause Postharvest Decay in Fruits." Molecular Plant-Microbe Interactions® 13, no. 8 (2000): 837–46. http://dx.doi.org/10.1094/mpmi.2000.13.8.837.

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A hexapeptide of amino acid sequence Ac-Arg-Lys-Thr-Trp-Phe-Trp-NH 2 was demonstrated to have antimicrobial activity against selected phytopathogenic fungi that cause postharvest decay in fruits. The peptide synthesized with either all D- or all L-amino acids inhibited the in vitro growth of strains of Penicillium italicum, P. digitatum, and Botrytis cinerea, with MICs of 60 to 80 μM and 50% inhibitory concentration (IC50) of 30 to 40 μM. The inhibitory activity of the peptide was both sequence- and fungus-specific since (i) sequence-related peptides lacked activity (including one with five re

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Tani, Naoki, Kohei Kazuma, Yukio Ohtsuka, et al. "Mass Spectrometry Analysis and Biological Characterization of the Predatory Ant Odontomachus monticola Venom and Venom Sac Components." Toxins 11, no. 1 (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 suc

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Nagarajan, Deepesh, Tushar Nagarajan, Neha Nanajkar, and Nagasuma Chandra. "A Uniform In Vitro Efficacy Dataset to Guide Antimicrobial Peptide Design." Data 4, no. 1 (2019): 27. http://dx.doi.org/10.3390/data4010027.

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Antimicrobial peptides are ubiquitous molecules that form the innate immune system of organisms across all kingdoms of life. Despite their prevalence and early origins, they continue to remain potent natural antimicrobial agents. Antimicrobial peptides are therefore promising drug candidates in the face of overwhelming multi-drug resistance to conventional antibiotics. Over the past few decades, thousands of antimicrobial peptides have been characterized in vitro, and their efficacy data are now available in a multitude of public databases. Computational antimicrobial peptide design attempts t

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Zorin, Evgeny A., Marina S. Kliukova, Olga A. Kulaeva, Alexey M. Afonin, Igor A. Tikhonovich, and Vladimir A. Zhukov. "Identification of sequences encoding for ncr-peptides and defensins in the ‘meta-assembly’ of transcriptome of pea (pisum sativum l.) Nitrogen-fixing nodules." Ecological genetics 17, no. 3 (2019): 39–46. http://dx.doi.org/10.17816/ecogen17339-46.

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Background. The active and careless applying of antibiotics in medicine and agriculture leads to the emergence of resistance to the existing antimicrobial drugs, which reduces the effectiveness of their use. One of the ways to solve this problem is the development of new antibiotics based on plant peptides with antimicrobial activity, for example plant defensins (which identified in all plants) and NCR peptides that are specifically synthesized in nodules of some leguminous plants. Materials and methods. In the present study, a meta-assembly of a transcriptome was constructed based on pu

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Michalek, Matthias, Bruno Vincent, Rainer Podschun, Joachim Grötzinger, Burkhard Bechinger, and Sascha Jung. "Hydramacin-1 in Action: Scrutinizing the Barnacle Model." Antimicrobial Agents and Chemotherapy 57, no. 7 (2013): 2955–66. http://dx.doi.org/10.1128/aac.02498-12.

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ABSTRACTHydramacin-1 (HM1) from the metazoanHydraexerts antimicrobial activity against a wide range of bacterial strains. Notably, HM1 induces the aggregation of bacterial cells, accompanied by precipitation. To date, the proposed mechanism of peptide-lipid interaction, termed the barnacle model, has not been described on the molecular level. Here, we show by biochemical and biophysical techniques that the lipid-peptide interactions of HM1 are initiated by electrostatic and hydrophobic effects, in particular, by tryptophan and neighboring polar amino acid residues that cause an interfacial loc

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Jenssen, Håvard, Pamela Hamill, and Robert E. W. Hancock. "Peptide Antimicrobial Agents." Clinical Microbiology Reviews 19, no. 3 (2006): 491–511. http://dx.doi.org/10.1128/cmr.00056-05.

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SUMMARY Antimicrobial host defense peptides are produced by all complex organisms as well as some microbes and have diverse and complex antimicrobial activities. Collectively these peptides demonstrate a broad range of antiviral and antibacterial activities and modes of action, and it is important to distinguish between direct microbicidal and indirect activities against such pathogens. The structural requirements of peptides for antiviral and antibacterial activities are evaluated in light of the diverse set of primary and secondary structures described for host defense peptides. Peptides wit

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Grishin, Sergei Y., Pavel A. Domnin, Sergey V. Kravchenko, et al. "Is It Possible to Create Antimicrobial Peptides Based on the Amyloidogenic Sequence of Ribosomal S1 Protein of P. aeruginosa?" International Journal of Molecular Sciences 22, no. 18 (2021): 9776. http://dx.doi.org/10.3390/ijms22189776.

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The development and testing of new antimicrobial peptides (AMPs) represent an important milestone toward the development of new antimicrobial drugs that can inhibit the growth of pathogens and multidrug-resistant microorganisms such as Pseudomonas aeruginosa, Gram-negative bacteria. Most AMPs achieve these goals through mechanisms that disrupt the normal permeability of the cell membrane, which ultimately leads to the death of the pathogenic cell. Here, we developed a unique combination of a membrane penetrating peptide and peptides prone to amyloidogenesis to create hybrid peptide: “cell pene

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Ball, S. L., G. P. Siou, J. A. Wilson, A. Howard, B. H. Hirst, and J. Hall. "Expression and immunolocalisation of antimicrobial peptides within human palatine tonsils." Journal of Laryngology & Otology 121, no. 10 (2007): 973–78. http://dx.doi.org/10.1017/s0022215107006184.

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Background: Recurrent acute tonsillitis is one of the most frequent ENT referrals, yet its pathogenesis remains poorly understood, and tonsillectomy still costs the National Health Service more than £60 000 000 annually. Antimicrobial cationic peptides are components of the innate immune system. They are generally small, highly positively charged peptides with broad spectrum antimicrobial activity which function as the body's ‘natural antibiotics'. The role of antimicrobial cationic peptides in the susceptibility of patients to recurrent acute tonsillitis is unknown.Aims: To characterise and c

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Kraszewska, Joanna, Michael C. Beckett, Tharappel C. James, and Ursula Bond. "Comparative Analysis of the Antimicrobial Activities of Plant Defensin-Like and Ultrashort Peptides against Food-Spoiling Bacteria." Applied and Environmental Microbiology 82, no. 14 (2016): 4288–98. http://dx.doi.org/10.1128/aem.00558-16.

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ABSTRACTAntimicrobial peptides offer potential as novel therapeutics to combat food spoilage and poisoning caused by pathogenic and nonpathogenic bacteria. Our previous studies identified the peptide human beta-defensin 3 (HBD3) as a potent antimicrobial agent against a wide range of beer-spoiling bacteria. Thus, HBD3 is an excellent candidate for development as an additive to prevent food and beverage spoilage. To expand the repertoire of peptides with antimicrobial activity against bacteria associated with food spoilage and/or food poisoning, we carried out anin silicodiscovery pipeline to i

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Strandberg, Erik, Deniz Tiltak, Marco Ieronimo, Nathalie Kanithasen, Parvesh Wadhwani та Anne S. Ulrich. "Influence of C-terminal amidation on the antimicrobial and hemolytic activities of cationic α-helical peptides". Pure and Applied Chemistry 79, № 4 (2007): 717–28. http://dx.doi.org/10.1351/pac200779040717.

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The effect of C-terminal amidation on the antimicrobial and hemolytic activities of antimicrobial peptides was studied using three cationic peptides which form amphiphilic α-helices when bound to membranes. The natural antimicrobial peptide PGLa, the designer-made antibiotic MSI-103, and the cell-penetrating "model amphipathic peptide" (MAP) are all amidated in their original forms, and their biological activities were compared with the same sequences carrying a free C-terminus. It was found that, in general, a free COOH-terminus reduces both the antimicrobial activity and the hemolytic side e

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Suryawanshi, Sunil Kumar, and Usha Chouhan. "COMPUTATIONAL APPROACHES FOR THE PREDICTION OF ANTIMICROBIAL POTENTIAL PEPTIDES FROM OCIMUM TENUIFLORUM." Asian Journal of Pharmaceutical and Clinical Research 11, no. 1 (2018): 398. http://dx.doi.org/10.22159/ajpcr.2017.v11i1.23008.

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Objective: In this study, antimicrobial activity was predicted against novel antimicrobial target 1SDE receptor to understand the structural feature of predicted peptides using machine learning approach from Ocimum tenuiflorum. Methods: Protein sequences from O. tenuiflorum were digested using peptide cutter and further processed for the prediction of antimicrobial peptide (AMP) through AMP predictor tool of CAMP which have multidimensional algorithms such as support vector machine, artificial neural network, random forest, and discriminant analysis. After analyzing various peptides, only four

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Suryawanshi, Sunil Kumar, and Usha Chouhan. "COMPUTATIONAL APPROACHES FOR THE PREDICTION OF ANTIMICROBIAL POTENTIAL PEPTIDES FROM OCIMUM TENUIFLORUM." Asian Journal of Pharmaceutical and Clinical Research 11, no. 1 (2018): 398. http://dx.doi.org/10.22159/ajpcr.2018.v11i1.23008.

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Objective: In this study, antimicrobial activity was predicted against novel antimicrobial target 1SDE receptor to understand the structural feature of predicted peptides using machine learning approach from Ocimum tenuiflorum. Methods: Protein sequences from O. tenuiflorum were digested using peptide cutter and further processed for the prediction of antimicrobial peptide (AMP) through AMP predictor tool of CAMP which have multidimensional algorithms such as support vector machine, artificial neural network, random forest, and discriminant analysis. After analyzing various peptides, only four

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Jung, Sook-In, Jonathan S. Finkel, Norma V. Solis, et al. "Bcr1 Functions Downstream of Ssd1 To Mediate Antimicrobial Peptide Resistance in Candida albicans." Eukaryotic Cell 12, no. 3 (2013): 411–19. http://dx.doi.org/10.1128/ec.00285-12.

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ABSTRACTIn order to colonize the host and cause disease,Candida albicansmust avoid being killed by host defense peptides. Previously, we determined that the regulatory protein Ssd1 governs antimicrobial peptide resistance inC. albicans. Here, we sought to identify additional genes whose products govern susceptibility to antimicrobial peptides. We discovered that abcr1Δ/Δ mutant, like thessd1Δ/Δ mutant, had increased susceptibility to the antimicrobial peptides, protamine, RP-1, and human β defensin-2. Homozygous deletion ofBCR1in thessd1Δ/Δ mutant did not result in a further increase in antimi

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Browne, Katrina, Sudip Chakraborty, Renxun Chen, et al. "A New Era of Antibiotics: The Clinical Potential of Antimicrobial Peptides." International Journal of Molecular Sciences 21, no. 19 (2020): 7047. http://dx.doi.org/10.3390/ijms21197047.

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Antimicrobial resistance is a multifaceted crisis, imposing a serious threat to global health. The traditional antibiotic pipeline has been exhausted, prompting research into alternate antimicrobial strategies. Inspired by nature, antimicrobial peptides are rapidly gaining attention for their clinical potential as they present distinct advantages over traditional antibiotics. Antimicrobial peptides are found in all forms of life and demonstrate a pivotal role in the innate immune system. Many antimicrobial peptides are evolutionarily conserved, with limited propensity for resistance. Additiona

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Haney, Evan F., Leonard T. Nguyen, David J. Schibli, and Hans J. Vogel. "Design of a novel tryptophan-rich membrane-active antimicrobial peptide from the membrane-proximal region of the HIV glycoprotein, gp41." Beilstein Journal of Organic Chemistry 8 (July 24, 2012): 1172–84. http://dx.doi.org/10.3762/bjoc.8.130.

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A number of physicochemical characteristics have been described which contribute to the biological activity of antimicrobial peptides. This information was used to design a novel antimicrobial peptide sequence by using an intrinsically inactive membrane-associated peptide derived from the HIV glycoprotein, gp41, as a starting scaffold. This peptide corresponds to the tryptophan-rich membrane-proximal region of gp41, which is known to interact at the interfacial region of the viral membrane and adopts a helical structure in the presence of lipids. Three synthetic peptides were designed to incre

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Lorenzón, E. N., G. F. Cespedes, E. F. Vicente, et al. "Effects of Dimerization on the Structure and Biological Activity of Antimicrobial Peptide Ctx-Ha." Antimicrobial Agents and Chemotherapy 56, no. 6 (2012): 3004–10. http://dx.doi.org/10.1128/aac.06262-11.

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ABSTRACTIt is well known that cationic antimicrobial peptides (cAMPs) are potential microbicidal agents for the increasing problem of antimicrobial resistance. However, the physicochemical properties of each peptide need to be optimized for clinical use. To evaluate the effects of dimerization on the structure and biological activity of the antimicrobial peptide Ctx-Ha, we have synthesized the monomeric and three dimeric (Lys-branched) forms of the Ctx-Ha peptide by solid-phase peptide synthesis using a combination of 9-fluorenylmethyloxycarbonyl (Fmoc) andt-butoxycarbonyl (Boc) chemical appro

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Xie, Zhipeng, Manchuriga Wang, and Yingxia Zhang. "Antimicrobial peptide database helps design novel antimicrobial peptides." Toxicon 158 (February 2019): S76. http://dx.doi.org/10.1016/j.toxicon.2018.10.259.

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Fleeman, Renee M., Luis A. Macias, Jennifer S. Brodbelt, and Bryan W. Davies. "Defining principles that influence antimicrobial peptide activity against capsulatedKlebsiella pneumoniae." Proceedings of the National Academy of Sciences 117, no. 44 (2020): 27620–26. http://dx.doi.org/10.1073/pnas.2007036117.

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The extracellular polysaccharide capsule ofKlebsiella pneumoniaeresists penetration by antimicrobials and protects the bacteria from the innate immune system. Host antimicrobial peptides are inactivated by the capsule as it impedes their penetration to the bacterial membrane. While the capsule sequesters most peptides, a few antimicrobial peptides have been identified that retain activity against encapsulatedK. pneumoniae,suggesting that this bacterial defense can be overcome. However, it is unclear what factors allow peptides to avoid capsule inhibition. To address this, we created a peptide

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Yeaman, Michael R., Kimberly D. Gank, Arnold S. Bayer, and Eric P. Brass. "Synthetic Peptides That Exert Antimicrobial Activities in Whole Blood and Blood-Derived Matrices." Antimicrobial Agents and Chemotherapy 46, no. 12 (2002): 3883–91. http://dx.doi.org/10.1128/aac.46.12.3883-3891.2002.

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ABSTRACT Peptides that exert antimicrobial activity in artificial media may lack activity within blood or other complex biological matrices. To facilitate the evaluation of antimicrobial peptides for possible therapeutic utility, an ex vivo assay was developed to assess the extent and durability of peptide antimicrobial activities in complex fluid biomatrices of whole blood, plasma, and serum compared with those in conventional media. Novel antimicrobial peptides (RP-1 and RP-11) were designed based in part on platelet microbicidal proteins. RP-1, RP-11, or gentamicin was introduced into bioma

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Ciociola, Tecla, Thelma A. Pertinhez, Laura Giovati, et al. "Dissecting the Structure-Function Relationship of a Fungicidal Peptide Derived from the Constant Region of Human Immunoglobulins." Antimicrobial Agents and Chemotherapy 60, no. 4 (2016): 2435–42. http://dx.doi.org/10.1128/aac.01753-15.

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ABSTRACTSynthetic peptides encompassing sequences related to the complementarity-determining regions of antibodies or derived from their constant region (Fc peptides) were proven to exert differential antimicrobial, antiviral, antitumor, and/or immunomodulatory activitiesin vitroand/orin vivo, regardless of the specificity and isotype of the parental antibody. Alanine substitution derivatives of these peptides exhibited unaltered, increased, or decreased candidacidal activitiesin vitro. The bioactive IgG-derived Fc N10K peptide (NQVSLTCLVK) spontaneously self-assembles, a feature previously re

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Racheva, M., O. Romero, K. K. Julich-Gruner, A. S. Ulrich, C. Wischke, and A. Lendlein. "Purity of mushroom tyrosinase as a biocatalyst for biomaterial synthesis affects the stability of therapeutic peptides." MRS Proceedings 1718 (2015): 85–90. http://dx.doi.org/10.1557/opl.2015.260.

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ABSTRACTThe formation of injectable implants in the presence of cells or solutes has previously been conceptualized to be based on the selectivity of bioorthogonal chemical reactions. As an alternative approach, hydrogel network synthesis by enzymatic reactions with a typically high inherent substrate specificity and low toxicity have been repeatedly proposed, e.g. using commercial mushroom tyrosinase (MTyr), which specifically catalyzes phenol oxidation. In this study, it should be explored whether MTyr is compatible with therapeutic peptides that may be delivered from such hydrogels in the f

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Gomes, Ana, Lucinda J. Bessa, Patrícia Correia, et al. "“Clicking” an Ionic Liquid to a Potent Antimicrobial Peptide: On the Route towards Improved Stability." International Journal of Molecular Sciences 21, no. 17 (2020): 6174. http://dx.doi.org/10.3390/ijms21176174.

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A covalent conjugate between an antibacterial ionic liquid and an antimicrobial peptide was produced via “click” chemistry, and found to retain the parent peptide’s activity against multidrug-resistant clinical isolates of Gram-negative bacteria, and antibiofilm action on a resistant clinical isolate of Klebsiella pneumoniae, while exhibiting much improved stability towards tyrosinase-mediated modifications. This unprecedented communication is a prelude for the promise held by ionic liquids -based approaches as tools to improve the action of bioactive peptides.

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Hitt, Samantha J., Barney M. Bishop, and Monique L. van Hoek. "Komodo-dragon cathelicidin-inspired peptides are antibacterial against carbapenem-resistant Klebsiella pneumoniae." Journal of Medical Microbiology 69, no. 11 (2020): 1262–72. http://dx.doi.org/10.1099/jmm.0.001260.

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Introduction. The rise of carbapenem-resistant enterobacteriaceae (CRE) is a growing crisis that requires development of novel therapeutics. Hypothesis. To this end, cationic antimicrobial peptides (CAMPs) represent a possible source of new potential therapeutics to treat difficult pathogens such as carbapenem-resistant Klebsiella pneumoniae (CRKP), which has gained resistance to many if not all currently approved antibiotics, making treatment difficult. Aim. To examine the anti-CRKP antimicrobial activity of the predicted cathelicidins derived from Varanus komodoensis (Komodo dragon) as well

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Audrain, Bianca, Lionel Ferrières, Amira Zairi, et al. "Induction of the Cpx Envelope Stress Pathway Contributes to Escherichia coli Tolerance to Antimicrobial Peptides." Applied and Environmental Microbiology 79, no. 24 (2013): 7770–79. http://dx.doi.org/10.1128/aem.02593-13.

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ABSTRACTAntimicrobial peptides produced by multicellular organisms as part of their innate system of defense against microorganisms are currently considered potential alternatives to conventional antibiotics in case of infection by multiresistant bacteria. However, while the mode of action of antimicrobial peptides is relatively well described, resistance mechanisms potentially induced or selected by these peptides are still poorly understood. In this work, we studied the mechanisms of action and resistance potentially induced by ApoEdpL-W, a new antimicrobial peptide derived from human apolip

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Wang, Guangshun. "Bioinformatic Analysis of 1000 Amphibian Antimicrobial Peptides Uncovers Multiple Length-Dependent Correlations for Peptide Design and Prediction." Antibiotics 9, no. 8 (2020): 491. http://dx.doi.org/10.3390/antibiotics9080491.

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Amphibians are widely distributed on different continents, except for the polar regions. They are important sources for the isolation, purification and characterization of natural compounds, including peptides with various functions. Innate immune antimicrobial peptides (AMPs) play a critical role in warding off invading pathogens, such as bacteria, fungi, parasites, and viruses. They may also have other biological functions such as endotoxin neutralization, chemotaxis, anti-inflammation, and wound healing. This article documents a bioinformatic analysis of over 1000 amphibian antimicrobial pe

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He, Dangui, Zhijian Cao, Ruhong Zhang, and Wenhua Li. "Molecular Cloning and Functional Identification of the Antimicrobial Peptide Gene Ctri9594 from the Venom of the Scorpion Chaerilus tricostatus." Antibiotics 10, no. 8 (2021): 896. http://dx.doi.org/10.3390/antibiotics10080896.

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Scorpion venom is a mixture of bioactive peptides, among which neurotoxins and antimicrobial peptides serve especially vital functions. Scorpion venom peptides in Buthidae species have been well described, but toxic peptides from non-Buthidae species have been under-investigated. Here, an antimicrobial peptide gene, Ctri9594, was cloned and functionally identified from the venom of the scorpion Chaerilus tricostatus. The precursor nucleotide sequence of Ctri9594 is 199 nt in length, including a 43 nt 5′ UTR, 115 nt 3′ UTR and 210 nt ORF. The ORF encodes 69 amino acid residues, containing a 21

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Wojciechowska, Monika, Joanna Miszkiewicz, and Joanna Trylska. "Conformational Changes of Anoplin, W-MreB1–9, and (KFF)3K Peptides near the Membranes." International Journal of Molecular Sciences 21, no. 24 (2020): 9672. http://dx.doi.org/10.3390/ijms21249672.

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Many peptides interact with biological membranes, but elucidating these interactions is challenging because cellular membranes are complex and peptides are structurally flexible. To contribute to understanding how the membrane-active peptides behave near the membranes, we investigated peptide structural changes in different lipid surroundings. We focused on two antimicrobial peptides, anoplin and W-MreB1–9, and one cell-penetrating peptide, (KFF)3K. Firstly, by using circular dichroism spectroscopy, we determined the secondary structures of these peptides when interacting with micelles, liposo

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Casciaro, Bruno, Floriana Cappiello, Maria Rosa Loffredo, Francesca Ghirga, and Maria Luisa Mangoni. "The Potential of Frog Skin Peptides for Anti-Infective Therapies: The Case of Esculentin-1a(1-21)NH2." Current Medicinal Chemistry 27, no. 9 (2020): 1405–19. http://dx.doi.org/10.2174/0929867326666190722095408.

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Antimicrobial Peptides (AMPs) are the key effectors of the innate immunity and represent promising molecules for the development of new antibacterial drugs. However, to achieve this goal, some problems need to be overcome: (i) the cytotoxic effects at high concentrations; (ii) the poor biostability and (iii) the difficulty in reaching the target site. Frog skin is one of the richest natural storehouses of AMPs, and over the years, many peptides have been isolated from it, characterized and classified into several families encompassing temporins, brevinins, nigrocins and esculentins. In this re

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Pini, Alessandro, Andrea Giuliani, Chiara Falciani, et al. "Antimicrobial Activity of Novel Dendrimeric Peptides Obtained by Phage Display Selection and Rational Modification." Antimicrobial Agents and Chemotherapy 49, no. 7 (2005): 2665–72. http://dx.doi.org/10.1128/aac.49.7.2665-2672.2005.

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ABSTRACT A large 10-mer phage peptide library was panned against whole Escherichia coli cells, and an antimicrobial peptide (QEKIRVRLSA) was selected. The peptide was synthesized in monomeric and dendrimeric tetrabranched form (multiple antigen peptide [MAP]), which generally allows a dramatic increase of peptide stability to peptidases and proteases. The antibacterial activity of the dendrimeric peptide against E. coli was much higher than that of the monomeric form. Modification of the original sequence, by residue substitution or sequence shortening, produced three different MAPs, M4 (QAKIR

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Almsned, Fahad. "Designing Antimicrobial Peptide: Current Status." Journal of Medical Science And clinical Research 05, no. 03 (2016): 19282–94. http://dx.doi.org/10.18535/jmscr/v5i3.153.

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Oyston, P. C. F., M. A. Fox, S. J. Richards, and G. C. Clark. "Novel peptide therapeutics for treatment of infections." Journal of Medical Microbiology 58, no. 8 (2009): 977–87. http://dx.doi.org/10.1099/jmm.0.011122-0.

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As antibiotic resistance increases worldwide, there is an increasing pressure to develop novel classes of antimicrobial compounds to fight infectious disease. Peptide therapeutics represent a novel class of therapeutic agents. Some, such as cationic antimicrobial peptides and peptidoglycan recognition proteins, have been identified from studies of innate immune effector mechanisms, while others are completely novel compounds generated in biological systems. Currently, only selected cationic antimicrobial peptides have been licensed, and only for topical applications. However, research using ne

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Zhang, Yong-lian, and Hsiao-Chang Chan. "S1h1-4 An epididymis-specific antimicrobial peptide has dual functions in sperm maturation(S1-h1 "Antimicrobial Peptides and Membrane Interactions",Symposia,Abstract,Meeting Program of EABS & BSJ 2006)." Seibutsu Butsuri 46, supplement2 (2006): S113. http://dx.doi.org/10.2142/biophys.46.s113_2.

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Bagheri, Mojtaba, Michael Beyermann, and Margitta Dathe. "Immobilization Reduces the Activity of Surface-Bound Cationic Antimicrobial Peptides with No Influence upon the Activity Spectrum." Antimicrobial Agents and Chemotherapy 53, no. 3 (2008): 1132–41. http://dx.doi.org/10.1128/aac.01254-08.

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ABSTRACT Early studies of immobilized peptides mainly focused upon the relationship between structural properties and the activity of soluble and surface-tethered sequences. The intention of this study was to analyze the influence of immobilization parameters upon the activity profile of peptides. Resin beads (TentaGel S NH2, HypoGel 400 NH2, and HypoGel 200 NH2) with polyethylene glycol spacers of different lengths were rendered antimicrobial by linkage of an amphipathic model KLAL peptide and magainin-derived MK5E. Standard solid-phase peptide synthesis, thioalkylation, and ligation strategi

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Wu, Qihui, Hanzhong Ke, Dongli Li, Qi Wang, Jiansong Fang, and Jingwei Zhou. "Recent Progress in Machine Learning-based Prediction of Peptide Activity for Drug Discovery." Current Topics in Medicinal Chemistry 19, no. 1 (2019): 4–16. http://dx.doi.org/10.2174/1568026619666190122151634.

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Over the past decades, peptide as a therapeutic candidate has received increasing attention in drug discovery, especially for antimicrobial peptides (AMPs), anticancer peptides (ACPs) and antiinflammatory peptides (AIPs). It is considered that the peptides can regulate various complex diseases which are previously untouchable. In recent years, the critical problem of antimicrobial resistance drives the pharmaceutical industry to look for new therapeutic agents. Compared to organic small drugs, peptide- based therapy exhibits high specificity and minimal toxicity. Thus, peptides are widely recr

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Deslouches, Berthony, Shruti M. Phadke, Vanja Lazarevic, et al. "De Novo Generation of Cationic Antimicrobial Peptides: Influence of Length and Tryptophan Substitution on Antimicrobial Activity." Antimicrobial Agents and Chemotherapy 49, no. 1 (2005): 316–22. http://dx.doi.org/10.1128/aac.49.1.316-322.2005.

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ABSTRACT Comparison of human immunodeficiency virus lentiviral lytic peptide 1 with other host-derived peptides indicates that antimicrobial properties of membrane-active peptides are markedly influenced by their cationic, hydrophobic, and amphipathic properties. Many common themes, such as Arg composition of the cationic face of an amphipathic helix and the importance of maintaining the hydrophobic face, have been deduced from these observations. These studies suggest that a peptide with these structural properties can be derived de novo by using only a few strategically positioned amino acid

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Tanaka, Tsuyoshi, Yoriko Kokuryu, and Tadashi Matsunaga. "Novel Method for Selection of Antimicrobial Peptides from a Phage Display Library by Use of Bacterial Magnetic Particles." Applied and Environmental Microbiology 74, no. 24 (2008): 7600–7606. http://dx.doi.org/10.1128/aem.00162-08.

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ABSTRACT Antimicrobial peptides were isolated from a phage display peptide library using bacterial magnetic particles (BacMPs) as a solid support. The BacMPs obtained from “Magnetospirillum magneticum” strain AMB-1 consist of pure magnetite (50 to 100 nm in size) and are covered with a lipid bilayer membrane derived from the invagination of the inner membrane. BacMPs are easily purified from a culture of magnetotactic bacteria by magnetic separation. Approximately 4 × 1010 PFU of the library phage (complexity, 2.7 × 109) was reacted with BacMPs. The elution of bound phages from BacMPs was perf

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Li, Bin, Peng Lyu, Shuping Xie, et al. "LFB: A Novel Antimicrobial Brevinin-Like Peptide from the Skin Secretion of the Fujian Large Headed Frog, Limnonectes fujianensi." Biomolecules 9, no. 6 (2019): 242. http://dx.doi.org/10.3390/biom9060242.

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Amphibians are a natural source of abundant antimicrobial peptides and thus have been widely investigated for isolation of such biomolecules. Many new antimicrobial peptide families have been discovered from amphibians. In this study, a novel antimicrobial peptide named Limnonectes fujianensis Brevinvin (LFB) has been identified in the skin secretion from the Fujian large headed frog, Limnonectes fujianensis. The cDNA sequence was cloned from a skin secretion library and the predicted mature peptide was identified through MS/MS fragmentation sequencing of reverse phase HPLC fractions on the sa

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Jin, Yi, Janet Hammer, Michelle Pate та ін. "Antimicrobial Activities and Structures of Two Linear Cationic Peptide Families with Various Amphipathic β-Sheet and α-Helical Potentials". Antimicrobial Agents and Chemotherapy 49, № 12 (2005): 4957–64. http://dx.doi.org/10.1128/aac.49.12.4957-4964.2005.

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ABSTRACT Many naturally occurring antimicrobial peptides comprise cationic linear sequences with the potential to adopt an amphipathic α-helical conformation. We designed a linear 18-residue peptide that adopted an amphipathic β-sheet structure when it was bound to lipids. In comparison to a 21-residue amphipathic α-helical peptide of equal charge and hydrophobicity, this peptide possessed more similar antimicrobial activity and greater selectivity in binding to and inducing leakage in vesicles composed of bacterial membrane lipids than vesicles composed of mammalian membrane lipids (J. Blazyk

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Cerrato, Andrea, Anna Laura Capriotti, Federico Capuano, et al. "Identification and Antimicrobial Activity of Medium-Sized and Short Peptides from Yellowfin Tuna (Thunnus albacares) Simulated Gastrointestinal Digestion." Foods 9, no. 9 (2020): 1185. http://dx.doi.org/10.3390/foods9091185.

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Due to the rapidly increasing resistance to conventional antibiotics, antimicrobial peptides are emerging as promising novel drug candidates. In this study, peptide fragments were obtained from yellowfin tuna muscle by simulated gastrointestinal digestion, and their antimicrobial activity towards Gram-positive and Gram-negative bacteria was investigated. In particular, the antimicrobial activity of both medium- and short-sized peptides was investigated by using two dedicated approaches. Medium-sized peptides were purified by solid phase extraction on C18, while short peptides were purified tha

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Chrom, Christina, Lindsay Renn, and Gregory Caputo. "Characterization and Antimicrobial Activity of Amphiphilic Peptide AP3 and Derivative Sequences." Antibiotics 8, no. 1 (2019): 20. http://dx.doi.org/10.3390/antibiotics8010020.

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The continued emergence of new antibiotic resistant bacterial strains has resulted in great interest in the development of new antimicrobial treatments. Antimicrobial peptides (AMPs) are one of many potential classes of molecules to help meet this emerging need. AMPs are naturally derived sequences, which act as part of the innate immune system of organisms ranging from insects through humans. We investigated the antimicrobial peptide AP3, which is originally isolated from the winter flounder Pleuronectes americanus. This peptide is of specific interest because it does not exhibit the canonica

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Kim, Young Soo, and Hyung Joon Cha. "High-Throughput and Facile Assay of Antimicrobial Peptides Using pH-Controlled Fluorescence Resonance Energy Transfer." Antimicrobial Agents and Chemotherapy 50, no. 10 (2006): 3330–35. http://dx.doi.org/10.1128/aac.00455-06.

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ABSTRACT Amphipathic antimicrobial peptides can destroy bacteria cells by inducing membrane permeabilization, forming one strategy for innate defense by various organisms. However, although the antimicrobial peptides are considered a promising alternative for use against multidrug-resistant bacteria, large-scale screening of potential candidate antimicrobial peptides will require a simple, rapid assay for antimicrobial activity. Here, we describe a novel fluorescence resonance energy transfer (FRET)-based assay system for antimicrobial peptides which takes advantage of pH-related changes in FR

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Avci, Fatma Gizem, Berna Sariyar Akbulut, and Elif Ozkirimli. "Membrane Active Peptides and Their Biophysical Characterization." Biomolecules 8, no. 3 (2018): 77. http://dx.doi.org/10.3390/biom8030077.

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In the last 20 years, an increasing number of studies have been reported on membrane active peptides. These peptides exert their biological activity by interacting with the cell membrane, either to disrupt it and lead to cell lysis or to translocate through it to deliver cargos into the cell and reach their target. Membrane active peptides are attractive alternatives to currently used pharmaceuticals and the number of antimicrobial peptides (AMPs) and peptides designed for drug and gene delivery in the drug pipeline is increasing. Here, we focus on two most prominent classes of membrane active

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Musin, Kh G. "ANTIMICROBIAL PEPTIDES — A POTENTIAL REPLACEMENT FOR TRADITIONAL ANTIBIOTICS." Russian Journal of Infection and Immunity 8, no. 3 (2018): 295–308. http://dx.doi.org/10.15789/2220-7619-2018-3-295-308.

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Antimicrobial peptides are a heterogeneous group of molecules involved in the innate and acquired immune response of various organisms, ranging from prokaryotes to mammals, including humans. They consist of 12–50 amino acid residues; have different physico-chemical and biological properties. The most common feature is their ability to destroy the prokaryotic cell membrane, which causes cell death. In the action, the molecules of antimicrobial peptides are embedded in the target bacteriological cells and change their conformation, forming structures in some cases resembling channels. Some other

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Cytryńska, Małgorzata, and Agnieszka Zdybicka-Barabas. "Defense peptides: recent developments." Biomolecular Concepts 6, no. 4 (2015): 237–51. http://dx.doi.org/10.1515/bmc-2015-0014.

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AbstractDefense peptides are small amphipathic molecules that exhibit antimicrobial, antitumor, antiviral, and immunomodulatory properties. This review summarizes current knowledge on the mechanisms of antimicrobial activity of cationic and anionic defense peptides, indicating peptide-based as well as microbial cell-based factors affecting this activity. The peptide-based factors include charge, hydrophibicity, and amphipathicity, whereas the pathogen-based factors are membrane lipid composition, presence of sterols, membrane fluidity, cell wall components, and secreted factors such as extrace

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Grafskaia, Ekaterina, Elizaveta Pavlova, Vladislav V. Babenko, et al. "The Hirudo Medicinalis Microbiome Is a Source of New Antimicrobial Peptides." International Journal of Molecular Sciences 21, no. 19 (2020): 7141. http://dx.doi.org/10.3390/ijms21197141.

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Antimicrobial peptides (AMPs) are considered a promising new class of anti-infectious agents. This study reports new antimicrobial peptides derived from the Hirudo medicinalis microbiome identified by a computational analysis method applied to the H. medicinalis metagenome. The identified AMPs possess a strong antimicrobial activity against Gram-positive and Gram-negative bacteria (MIC range: 5.3 to 22.4 μM), including Staphylococcus haemolyticus, an opportunistic coagulase–negative pathogen. The secondary structure analysis of peptides via CD spectroscopy showed that all the AMPs except pept_

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He, Jian, Randal Eckert, Thanh Pharm, et al. "Novel Synthetic Antimicrobial Peptides against Streptococcus mutans." Antimicrobial Agents and Chemotherapy 51, no. 4 (2007): 1351–58. http://dx.doi.org/10.1128/aac.01270-06.

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ABSTRACT Streptococcus mutans, a common oral pathogen and the causative agent of dental caries, has persisted and even thrived on the tooth surface despite constant removal and eradication efforts. In this study, we generated a number of synthetic antimicrobial peptides against this bacterium via construction and screening of several structurally diverse peptide libraries where the hydrophobicity and charge within each library was varied incrementally in order to generate a collection of peptides with different biochemical characteristics. From these libraries, we identified multiple peptides

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