APD2: the updated antimicrobial peptide database and its application in peptide design

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ID: 300644
2008
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Abstract
The antimicrobial peptide database (APD, http://aps.unmc.edu/AP/main.php) has been updated and expanded. It now hosts 1228 entries with 65 anticancer, 76 antiviral (53 anti-HIV), 327 antifungal and 944 antibacterial peptides. The second version of our database (APD2) allows users to search peptide families (e.g. bacteriocins, cyclotides, or defensins), peptide sources (e.g. fish, frogs or chicken), post-translationally modified peptides (e.g. amidation, oxidation, lipidation, glycosylation or d-amino acids), and peptide binding targets (e.g. membranes, proteins, DNA/RNA, LPS or sugars). Statistical analyses reveal that the frequently used amino acid residues (>10%) are Ala and Gly in bacterial peptides, Cys and Gly in plant peptides, Ala, Gly and Lys in insect peptides, and Leu, Ala, Gly and Lys in amphibian peptides. Using frequently occurring residues, we demonstrate database-aided peptide design in different ways. Among the three peptides designed, GLK-19 showed a higher activity against Escherichia coli than human LL-37.
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openalex_W1977241485 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Guangshun Wang, Xia Li, Zhe Wang
Journal Nucleic Acids Research
Year 2008
DOI
10.1093/nar/gkn823
URL
https://academic.oup.com/nar/article-pdf/37/suppl_1/D933/16758395/gkn823.pdf
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