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The Antimicrobial Peptide Database (APD) contains 3251 antimicrobial peptides from six kingdoms (365 bacteriocins/peptide antibiotics from bacteria, 5 from archaea, 8 from protists, 21 from fungi, 360 from plants, and 2409 from animals, including some synthetic peptides) with the following activity:
Antibacterial peptides; Antibiofilm peptides;
Anti-MRSA peptides; Anti-TB peptidesNew;
Anti-endotoxin peptidesNew; Anti-toxin peptides;
Antiviral peptides; Anti-HIV peptides;
Antifungal peptides; Anti-Candida peptidesNew;
Antiparasitic peptides; Antimalarial peptides;
Anticancer peptides;
Anti-diabetic peptidesNew;
Wound healing peptides;
Chemotactic peptides; Anti-inflammatory peptides ;
Spermicidal peptides;
Insecticidal peptides;
Ion channel inhibitors;
Protease inhibitors;
Antioxidant peptides;
Surface immobilized peptides;
Two-chain peptides;
Synergistic peptides.
This original database for antimicrobial peptides is manually curated based on a set of data-collection criteria. There are 141 human host defense peptides, 328 from mammals annotated, 1117 active peptides from amphibians (1039 from frogs and 74 from toads), 136 fish peptides, 45 reptile peptides, 43 from birds, 577 from arthropods, [323 from insects, 71 from crustaceans, 8 from myriapods, 175 from chelicerata, (43 from spiders, 88 from scorpions)], 47 from molluscs, 6 AMPs from protozoa, and more.

This comprehensive database consists of a pipeline of search functions for innate immune peptides. You can search for peptide information using APD ID, peptide name, amino acid sequence, peptide motif, chemical modification, length, charge, hydrophobic content, PDB ID, 3D structure, methods for structural determination, peptide source organism, peptide family name, life domain/kingdom (bacteria, archaea, protists, fungi, plants, animals), biological activity (see the links above), synergistic effects, target microbes, molecular targets, mechanism of action, contributing authors, and year of publication.

Of the 443 unique NMR/X-ray diffracted 3D structures annotated for host defense peptides in the APD, 317 with coordinates deposited in the Protein Data Bank (PDB) can be directly rotated, zoomed, and viewed. Top left: Amphibian α-helical magainin II; Top right: bovine β-sheet lactoferricin; Bottom left: plant αβ-PsD1; Bottom right: bovine non-αβ indolicidin.

Important notice: 2020 FASTA sequence release has been sorted and uploaded for download.

CITE:
[1] Wang, G., Li, X. and Wang, Z. (2016) APD3: the antimicrobial peptide database as a tool for research and education. Nucleic Acids Research 44, D1087-D1093. Paper PDF
[2] Wang, G., Li, X. and Wang, Z. (2009) APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Research 37, D933-D937. Paper PDF
[3] Wang, Z. and Wang, G. (2004) APD: the antimicrobial peptide database. Nucleic Acids Research 32, D590-D592. Paper PDF

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Last updated: Oct 23, 2020 | Copyright 2003-2020 Dept of Pathology & Microbiology, UNMC, All Rights Reserved
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