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 2812 antimicrobial peptides from six kingdoms (297 bacteriocins and peptide antibiotics from bacteria, 4 from archaea, 8 from protists, 13 from fungi, 343 from plants, and 2147 from animals) with the following activity (Total AMPs: 2889):
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 (see About). There are 122 human host defense peptides, 1037 active peptides from amphibians (973 from frogs), 113 fish peptides, 32 reptile peptides, 38 from birds, 499 from arthropods, 150 from chelicerata, 53 from crustaceans, 7 from myriapods, 283 from insects, 43 from spiders, 77 from scorpions, 36 from molluscs; and more. A Universal Bacterial Peptide Nomenclature; A Unified Peptide Classification

Of the 386 unique 3D structures annotated for host defense peptides in the APD, 272 with coordinates deposited in the Protein Data Bank (PDB) can be directly rotated, zoomed, and viewed. Top left: Amphibian magainin II; Top right: bovine lactoferricin; Bottom left: plant PsD1; Bottom right: bovine indolicidin. A unified Peptide 3D Structure Classification

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.
Antimicrobial Peptides in 2014; AMPs as antibiotics

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

7479
Last updated: June 13, 2017 | Copyright 2003-2017 Dept of Pathology & Microbiology, UNMC, All Rights Reserved
space