The Database of Antimicrobial Activity and Structure of Peptides (DBAASP) has been created to provide users with information on detailed chemical structure and activity for those peptides which antimicrobial activity against particular targets have been evaluated experimentally. The database is manually curated and contains information on ribosomal, nonribosomal and synthetic peptides that show antimicrobial activity as Monomers, Multimers and Multi-Peptides.

Monomer - consists of one polypeptide chain (for example: Melittin, Magainin).

Multimer - consists of two or more polypeptide chains with interchain covalent bond(s) (for example: Distinctin, Halocidin).

Multi-Peptide - consists of two or more different polypeptide chains without interchain covalent bond. Their complete antimicrobial activity requires the synergistic action of the peptides in equimolar concentrations, the individual peptides have little or no activity (for example: Enterocin X, Salivaricin P).

Project initially was supported by Shota Rustaveli National Science Foundation (GEORGIA) and Centre National de la Recherche Scientifique (FRANCE).

Now it is a joint project of Laboratory of Bioinformatics of Ivane Beritashvili Center of Experimental Biomedicine (IBCEB, GEORGIA) and Office of Cyber Infrastructure and Computational Biology (OCICB/NIAID/NIH, USA)

People involved from IBCEB:

M. Pirtskhalava (
B. Vishnepolsky (
M. Grigolava (
M. Chubinidze (
E. Alimbarashvili (

People involved from NIAID:

A. Gabrielian (
M. Tartakovsky (
A. Rosental (
D. Hurt (
V. Alekseev (
P. Cruz (
A. Armstrong (