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BioMed Research International
Volume 2015 (2015), Article ID 475062, 6 pages
Resource Review

A Large-Scale Structural Classification of Antimicrobial Peptides

Department of Computer Science and Engineering, National Taiwan Ocean University, Keelung 202, Taiwan

Received 1 September 2014; Accepted 23 February 2015

Academic Editor: Oliver Ray

Copyright © 2015 Hao-Ting Lee et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Antimicrobial peptides (AMPs) are potent drug candidates against microbial organisms such as bacteria, fungi, parasites, and viruses. AMPs have abundant sequences and structures, two fundamental resources for bioinformatics researches, but analyses on how they associate with each other are either nonexistent or limited to partial classification and data. We thus present A Database of Anti-Microbial peptides (ADAM), which contains 7,007 unique sequences and 759 structures, to systematically establish comprehensive associations between AMP sequences and structures through structural folds and to provide an easy access to view their relationships. 30 distinct AMP structural fold clusters with more than one structure are detected and about a thousand AMPs are associated with at least one structural fold cluster. According to ADAM, AMP structural folds are limited—AMPs only cover about 3% of the overall protein fold space.