As of Jan 2024, the Antimicrobial Peptide Database (APD) contains 3940 peptides, including 3146 natural antimicrobial peptides (AMPs) from the six life kingdoms (383 bacteriocins/peptide antibiotics from bacteria, 5 from archaea, 8 from protists, 29 from fungi, 250 from plants, and 2463 from animals), 190 predicted and 314 synthetic AMPs 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. Among the natural AMPs with know antimicrobial activity, there are 144 human host defense peptides, 373 from mammals annotated, 1079 active peptides from amphibians (1006 from frogs and 68 from toads), 146 fish peptides, 52 reptile peptides, 47 from birds, 619 from arthropods, [364 from insects, 70 from crustaceans, 7 from myriapods, 178 from chelicerata, (38 from spiders, 97 from scorpions)], 54 from molluscs, 6 AMPs from protozoa, and more.

Of the 486 unique 425 NMR/ 61 X-ray diffracted 3D structures annotated for host defense peptides in the APD, 343 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: Please indicate Dec 2023 when using the annual summary of AMP statistics on this page. For updated information in 2024, search the APD.

Invitation: We invite you to submit your next manuscripts to a Special Issue in Peptides covering all topics of AMPs (deadline May 2024)

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 2024 | Copyright 2003-2024 Dept of Pathology, Microbiology & Immunology, UNMC, All Rights Reserved

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