title banner reads
About | Database Search | Calculation & Prediction | Peptide Design | Statistics | AMP Facts | Contact
| AMP Timeline | Nomenclature | Classification | 3D Structure | My Tools| Seq Download| FAQs | APD News|
Glossary | Links | Opportunities| Conference| AMP News
The Antimicrobial Peptide Database (APD) contains 3011 antimicrobial peptides from six kingdoms (335 bacteriocins/peptide antibiotics from bacteria, 4 from archaea, 8 from protists, 16 from fungi, 343 from plants, and 2219 from animals, including some synthetic peptides) with the following activity:
Antibacterial peptides; Antibiofilm peptides
Antiviral peptides; Anti-HIV peptides
Antifungal peptides
Antiparasitic peptides; Antimalarial peptides
Anti-protist peptides
Anticancer peptides
Antioxidant peptides
Chemotactic peptides
Insecticidal peptides
Protease inhibitors
Spermicidal peptides
Surface immobilized peptides
Wound healing peptides
This comprehensive database for antimicrobial peptides is manually curated based on a set of data-collection criteria. There are 125 human host defense peptides, 280 from mammals annotated, 1065 active peptides from amphibians (996 from frogs), 122 fish peptides, 38 reptile peptides, 40 from birds, 525 from arthropods, [295 from insects, 59 from crustaceans, 7 from myriapods, 165 from chelicerata, (43 from spiders, 82 from scorpions)], 42 from molluscs, 6 AMPs from protozoa, and more.

Of the 402 unique 3D NMR/crystal structures annotated for host defense peptides in the APD, 283 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

14700741
Last updated: Aug 15, 2018 | Copyright 2003-2018 Dept of Pathology & Microbiology, UNMC, All Rights Reserved
space