Cargando…

ADAPTABLE: a comprehensive web platform of antimicrobial peptides tailored to the user’s research

Antimicrobial peptides (AMPs) are part of the innate immune response to pathogens in all of the kingdoms of life. They have received significant attention because of their extraordinary variety of activities, in particular, as candidate drugs against the threat of super-bacteria. A systematic study...

Descripción completa

Detalles Bibliográficos
Autores principales: Ramos-Martín, Francisco, Annaval, Thibault, Buchoux, Sébastien, Sarazin, Catherine, D’Amelio, Nicola
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Life Science Alliance LLC 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6864362/
https://www.ncbi.nlm.nih.gov/pubmed/31740563
http://dx.doi.org/10.26508/lsa.201900512
_version_ 1783471869693788160
author Ramos-Martín, Francisco
Annaval, Thibault
Buchoux, Sébastien
Sarazin, Catherine
D’Amelio, Nicola
author_facet Ramos-Martín, Francisco
Annaval, Thibault
Buchoux, Sébastien
Sarazin, Catherine
D’Amelio, Nicola
author_sort Ramos-Martín, Francisco
collection PubMed
description Antimicrobial peptides (AMPs) are part of the innate immune response to pathogens in all of the kingdoms of life. They have received significant attention because of their extraordinary variety of activities, in particular, as candidate drugs against the threat of super-bacteria. A systematic study of the relation between the sequence and the mechanism of action is urgently needed, given the thousands of sequences already in multiple web resources. ADAPTABLE web platform (http://gec.u-picardie.fr/adaptable) introduces the concept of “property alignment” to create families of property and sequence-related peptides (SR families). This feature provides the researcher with a tool to select those AMPs meaningful to their research from among more than 40,000 nonredundant sequences. Selectable properties include the target organism and experimental activity concentration, allowing selection of peptides with multiple simultaneous actions. This is made possible by ADAPTABLE because it not only merges sequences of AMP databases but also merges their data, thereby standardizing values and handling non-proteinogenic amino acids. In this unified platform, SR families allow the creation of peptide scaffolds based on common traits in peptides with similar activity, independently of their source.
format Online
Article
Text
id pubmed-6864362
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher Life Science Alliance LLC
record_format MEDLINE/PubMed
spelling pubmed-68643622019-11-21 ADAPTABLE: a comprehensive web platform of antimicrobial peptides tailored to the user’s research Ramos-Martín, Francisco Annaval, Thibault Buchoux, Sébastien Sarazin, Catherine D’Amelio, Nicola Life Sci Alliance Resources Antimicrobial peptides (AMPs) are part of the innate immune response to pathogens in all of the kingdoms of life. They have received significant attention because of their extraordinary variety of activities, in particular, as candidate drugs against the threat of super-bacteria. A systematic study of the relation between the sequence and the mechanism of action is urgently needed, given the thousands of sequences already in multiple web resources. ADAPTABLE web platform (http://gec.u-picardie.fr/adaptable) introduces the concept of “property alignment” to create families of property and sequence-related peptides (SR families). This feature provides the researcher with a tool to select those AMPs meaningful to their research from among more than 40,000 nonredundant sequences. Selectable properties include the target organism and experimental activity concentration, allowing selection of peptides with multiple simultaneous actions. This is made possible by ADAPTABLE because it not only merges sequences of AMP databases but also merges their data, thereby standardizing values and handling non-proteinogenic amino acids. In this unified platform, SR families allow the creation of peptide scaffolds based on common traits in peptides with similar activity, independently of their source. Life Science Alliance LLC 2019-11-18 /pmc/articles/PMC6864362/ /pubmed/31740563 http://dx.doi.org/10.26508/lsa.201900512 Text en © 2019 Ramos-Martín et al. https://creativecommons.org/licenses/by/4.0/This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).
spellingShingle Resources
Ramos-Martín, Francisco
Annaval, Thibault
Buchoux, Sébastien
Sarazin, Catherine
D’Amelio, Nicola
ADAPTABLE: a comprehensive web platform of antimicrobial peptides tailored to the user’s research
title ADAPTABLE: a comprehensive web platform of antimicrobial peptides tailored to the user’s research
title_full ADAPTABLE: a comprehensive web platform of antimicrobial peptides tailored to the user’s research
title_fullStr ADAPTABLE: a comprehensive web platform of antimicrobial peptides tailored to the user’s research
title_full_unstemmed ADAPTABLE: a comprehensive web platform of antimicrobial peptides tailored to the user’s research
title_short ADAPTABLE: a comprehensive web platform of antimicrobial peptides tailored to the user’s research
title_sort adaptable: a comprehensive web platform of antimicrobial peptides tailored to the user’s research
topic Resources
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6864362/
https://www.ncbi.nlm.nih.gov/pubmed/31740563
http://dx.doi.org/10.26508/lsa.201900512
work_keys_str_mv AT ramosmartinfrancisco adaptableacomprehensivewebplatformofantimicrobialpeptidestailoredtotheusersresearch
AT annavalthibault adaptableacomprehensivewebplatformofantimicrobialpeptidestailoredtotheusersresearch
AT buchouxsebastien adaptableacomprehensivewebplatformofantimicrobialpeptidestailoredtotheusersresearch
AT sarazincatherine adaptableacomprehensivewebplatformofantimicrobialpeptidestailoredtotheusersresearch
AT damelionicola adaptableacomprehensivewebplatformofantimicrobialpeptidestailoredtotheusersresearch