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The Antimicrobial Peptide Database (APD) contains 3140 antimicrobial peptides from six kingdoms (345 bacteriocins/peptide antibiotics from bacteria, 5 from archaea, 8 from protists, 20 from fungi, 352 from plants, and 2329 from animals, including some synthetic peptides) with the following activity:
Antibacterial peptides; Antibiofilm peptides; Anti-MRSA peptides;
Antiviral peptides; Anti-HIV peptides
Antifungal peptides; Anti-protist peptides
Antiparasitic peptides; Antimalarial peptides
Anticancer peptides
Spermicidal peptides
Insecticidal peptides
Chemotactic peptides; Anti-inflammatory peptides ; Wound healing peptides
Ion channel inhibitors
Anti-toxin peptides
Protease inhibitors
Antioxidant peptides
Surface immobilized peptides
This comprehensive database for antimicrobial peptides is manually curated based on a set of data-collection criteria. There are 135 human host defense peptides, 295 from mammals annotated, 1087 active peptides from amphibians (1018 from frogs), 133 fish peptides, 45 reptile peptides, 42 from birds, 556 from arthropods, [310 from insects, 66 from crustaceans, 7 from myriapods, 171 from chelicerata, (43 from spiders, 88 from scorpions)], 45 from molluscs, 6 AMPs from protozoa, and more.

Of the 428 unique NMR/X-ray diffracted 3D structures annotated for host defense peptides in the APD, 297 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 original 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.

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: Nov 20, 2019 | Copyright 2003-2019 Dept of Pathology & Microbiology, UNMC, All Rights Reserved
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