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Discovery of modulators of HIV-1 infection from the human peptidome

Almost all human proteins are subject to proteolytic degradation, which produces a broad range of peptides that have highly specific and sometimes unexpected functions. Peptide libraries that have been generated from human bodily fluids or tissues are a rich but mostly unexplored source of bioactive...

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Autores principales: Münch, Jan, Ständker, Ludger, Forssmann, Wolf-Georg, Kirchhoff, Frank
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7097597/
https://www.ncbi.nlm.nih.gov/pubmed/25110191
http://dx.doi.org/10.1038/nrmicro3312
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author Münch, Jan
Ständker, Ludger
Forssmann, Wolf-Georg
Kirchhoff, Frank
author_facet Münch, Jan
Ständker, Ludger
Forssmann, Wolf-Georg
Kirchhoff, Frank
author_sort Münch, Jan
collection PubMed
description Almost all human proteins are subject to proteolytic degradation, which produces a broad range of peptides that have highly specific and sometimes unexpected functions. Peptide libraries that have been generated from human bodily fluids or tissues are a rich but mostly unexplored source of bioactive compounds that could be used to develop antimicrobial and immunomodulatory therapeutic agents. In this Innovation article, we describe the discovery, optimization and application of endogenous bioactive peptides from human-derived peptide libraries, with a particular focus on the isolation of endogenous inhibitors and promoters of HIV-1 infection. SUPPLEMENTARY INFORMATION: The online version of this article (doi:10.1038/nrmicro3312) contains supplementary material, which is available to authorized users.
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spelling pubmed-70975972020-03-26 Discovery of modulators of HIV-1 infection from the human peptidome Münch, Jan Ständker, Ludger Forssmann, Wolf-Georg Kirchhoff, Frank Nat Rev Microbiol Article Almost all human proteins are subject to proteolytic degradation, which produces a broad range of peptides that have highly specific and sometimes unexpected functions. Peptide libraries that have been generated from human bodily fluids or tissues are a rich but mostly unexplored source of bioactive compounds that could be used to develop antimicrobial and immunomodulatory therapeutic agents. In this Innovation article, we describe the discovery, optimization and application of endogenous bioactive peptides from human-derived peptide libraries, with a particular focus on the isolation of endogenous inhibitors and promoters of HIV-1 infection. SUPPLEMENTARY INFORMATION: The online version of this article (doi:10.1038/nrmicro3312) contains supplementary material, which is available to authorized users. Nature Publishing Group UK 2014-08-11 2014 /pmc/articles/PMC7097597/ /pubmed/25110191 http://dx.doi.org/10.1038/nrmicro3312 Text en © Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. 2014 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Article
Münch, Jan
Ständker, Ludger
Forssmann, Wolf-Georg
Kirchhoff, Frank
Discovery of modulators of HIV-1 infection from the human peptidome
title Discovery of modulators of HIV-1 infection from the human peptidome
title_full Discovery of modulators of HIV-1 infection from the human peptidome
title_fullStr Discovery of modulators of HIV-1 infection from the human peptidome
title_full_unstemmed Discovery of modulators of HIV-1 infection from the human peptidome
title_short Discovery of modulators of HIV-1 infection from the human peptidome
title_sort discovery of modulators of hiv-1 infection from the human peptidome
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7097597/
https://www.ncbi.nlm.nih.gov/pubmed/25110191
http://dx.doi.org/10.1038/nrmicro3312
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