Welcome to the APD, the original database for antimicrobial peptides, first online in 2003. As of January 2025, the Antimicrobial Peptide Database (APD) contains 5099 peptides, including 3306 natural antimicrobial peptides (AMPs) from the six life kingdoms (410 bacteriocins/peptide antibiotics from bacteria, 5 from archaea, 8 from protists, 29 from fungi, 268 from plants, and 2580 from animals), 1299 synthetic, and 231 predicted AMPs with the following function/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 Nematocidal peptides bacteria-agglutinating peptides Synergistic peptides

This database is manually curated based on a set of data-collection criteria first defined in 2011. Among the 3306 natural AMPs with known sequence and activity, there are 154 human host defense peptides, 397 from mammals, 1110 active peptides from amphibians (1033 from frogs and 69 from toads), 150 fish peptides, 55 reptile peptides, 47 from birds, 677 from arthropods, [397 from insects, 73 from crustaceans, 7 from myriapods, 200 from chelicerata, (45 from spiders, 104 from scorpions)], 54 from molluscs, 6 AMPs from protozoa, and more.

Of the 523 unique 460 NMR/ 63 X-ray diffracted 3D structures annotated for host defense peptides in the APD, over 362 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 "as of December 2024" when you use the APD annual statistics of natural AMPs posted here. For an updated count during 2025, please search the database.

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 2025 | Copyright 2003-present Dept of Pathology, Microbiology & Immunology, UNMC, All Rights Reserved

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