The Antimicrobial Peptide Database (APD) contains 3569 antimicrobial peptides from six life kingdoms (380 isolated/predicted bacteriocins/peptide antibiotics from bacteria, 5 from archaea, 8 from protists, 25 from fungi, 371 from plants, and 2600 from animals, including genome-predicted and some synthetic peptides) with the following activity:

Antibacterial peptides Antibiofilm peptides Anti-MRSA peptides Anti-TB peptides Anti-endotoxin peptides Anti-toxin peptides Antiviral peptides Anti-HIV peptides Antifungal peptides Anti-Candida peptides Antiparasitic peptides Antimalarial peptides Anticancer peptides Anti-diabetic peptides 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 153 human host defense peptides, 363 from mammals annotated, 1196 active peptides from amphibians (1117 from frogs and 75 from toads), 144 fish peptides, 49 reptile peptides, 45 from birds, 633 from arthropods, [367 from insects, 75 from crustaceans, 8 from myriapods, 183 from chelicerata, (44 from spiders, 93 from scorpions)], 52 from molluscs, 6 AMPs from protozoa, and more.

Of the 457 unique 399 NMR/ 58 X-ray diffracted 3D structures annotated for host defense peptides in the APD, 326 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.

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.

Note: Indicate Jan 2023 when using the AMP numbers on this page. For updated information, search the APD.

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

Last updated: Jan 2023 | Copyright 2003-2023 Dept of Pathology & Microbiology, UNMC, All Rights Reserved

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