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Antimicrobial peptides

About: Antimicrobial peptides is a research topic. Over the lifetime, 10645 publications have been published within this topic receiving 507688 citations. The topic is also known as: host defense peptide & antimicrobial protein.


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Book ChapterDOI
TL;DR: In this article, the authors explored elements of the physical and chemical defense barriers of the cervicovaginal mucosa, which protect against infections of the lower genital tract, including the defensin family of peptides as well as polypeptides that are active against viruses such as HIV-1.
Abstract: Host defense responses of the human female genital tract mucosa to pathogenic microbes and viruses are mediated in part by the release of antimicrobial substances into the overlying mucosal fluid. While host defense has long been considered a prominent function of vaginal and cervical mucosae, evidence that cationic antimicrobial peptides and proteins have fundamental roles in the innate host defense of this tissue has only recently become available. This chapter explores elements of the physical and chemical defense barriers of the cervicovaginal mucosa, which protect against infections of the lower genital tract. Cationic antimicrobial and antiviral polypeptide components of cervicovaginal fluid are discussed in detail, with special emphasis placed on the defensin family of peptides as well as polypeptides that are active against viruses such as HIV-1. The reader should be cognizant that each polypeptide by itself does not provide complete protection of the genital tract. On the contrary, the abundance and multiplicity of antimicrobial peptides and proteins suggest protection of the cervicovaginal mucosa may be best realized from the aggregate effector molecules.

140 citations

Journal ArticleDOI
TL;DR: Recent efforts to create polymers which display biological activity similar to natural proteins, including antimicrobial and cell-penetrating peptides are presented.
Abstract: Natural macromolecules exhibit an extensive arsenal of properties, many of which have proven difficult to recapitulate in simpler synthetic systems. Over the last couple of years, foldamers have emerged as one important step toward increased functionality in synthetic systems. While the great majority of work in this area has focused on folded structures, hence the name, more recent progress has centered on polymers that mimic protein function. These efforts have resulted in the design of relatively simple macromolecules; one example are the synthetic mimics of antimicrobial peptides (SMAMPs) that capture the central physicochemical features of their natural archetypes irrespective of the specific folded form. Here we present our recent efforts to create polymers which display biological activity similar to natural proteins, including antimicrobial and cell-penetrating peptides.

140 citations

Journal ArticleDOI
TL;DR: This study found that exposure of keratinocytes cultured from a number of individuals to S. aureus resulted in approximately 2-3 log better killing than by HaCaT cells within 1 hour, indicating an essential role for beta-defensin 3 in the constitutive killing of bacteria by normal keratinocyte.

140 citations

Journal ArticleDOI
TL;DR: By offering a competitive advantage during colonization of the human body, the characteristically high production of PSMs in USA300 and other CA-MRSA strains may contribute not only to virulence but also the exceptional capacity of those strains to sustainably spread in the population, which so far has remained poorly understood.

139 citations

Journal ArticleDOI
01 Oct 2015-Peptides
TL;DR: This review outlines selected anion and cationic AMPs which are at various stages of development, from preliminary analysis to clinical drug development, and considers current production methods and delivery tools for AMPs, which must be improved for the effective use of these agents.

139 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023512
20221,025
2021809
2020844
2019728
2018634