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The Antimicrobial Peptide Database (APD) contains 3230 antimicrobial peptides from six kingdoms (358 bacteriocins/peptide antibiotics from bacteria, 5 from archaea, 8 from protists, 20 from fungi, 360 from plants, and 2396 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 peptides;
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; and Surface immobilized peptides.
This comprehensive database for antimicrobial peptides is manually curated based on a set of data-collection criteria. There are 141 human host defense peptides, 314 from mammals annotated, 1111 active peptides from amphibians (1031 from frogs, 76 from toads, and 4 from salamanders), 136 fish peptides, 45 reptile peptides, 43 from birds, 572 from arthropods, [319 from insects, 70 from crustaceans, 8 from myriapods, 175 from chelicerata, (43 from spiders, 88 from scorpions)], 47 from molluscs, 6 AMPs from protozoa, and more.

Of the 442 unique NMR/X-ray diffracted 3D structures annotated for host defense peptides in the APD, 315 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: Aug 4, 2020 | Copyright 2003-2020 Dept of Pathology & Microbiology, UNMC, All Rights Reserved
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