The antimicrobial peptide database provides a platform for decoding the design principles of naturally occurring antimicrobial peptides.
antimicrobial peptides
classification
database tool
peptide design
peptide signature
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
01 2020
01 2020
Historique:
received:
27
06
2019
revised:
23
07
2019
accepted:
24
07
2019
pubmed:
31
7
2019
medline:
22
9
2020
entrez:
31
7
2019
Statut:
ppublish
Résumé
This article is written for the 2020 tool issue of Protein Science. It briefly introduces the widely used antimicrobial peptide database, initially online in 2003. After a description of the main features of each database version and some recent additions, the focus is on the peptide design parameters for each of the four unified classes of natural antimicrobial peptides (AMPs). The amino acid signature in AMPs varies substantially, leading to a variety of structures for functional and mechanistic diversity. Also, Nature is a master of combinatorial chemistry by deploying different amino acids onto the same structural scaffold to tune peptide functions. In addition, the single-domain AMPs may be posttranslationally modified, self-assembled, or combined with other AMPs for function. Elucidation of the design principles of natural AMPs will facilitate future development of novel molecules for various applications.
Identifiants
pubmed: 31361941
doi: 10.1002/pro.3702
pmc: PMC6933855
doi:
Substances chimiques
Anti-Infective Agents
0
Peptides
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
8-18Subventions
Organisme : NIAID NIH HHS
ID : R01 AI105147
Pays : United States
Organisme : NIH HHS
ID : R01AI105147
Pays : United States
Informations de copyright
© 2019 The Protein Society.
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