PredSTP: a highly accurate SVM based model to predict sequential cystine stabilized peptides.

Journal: BMC bioinformatics
PMID:

Abstract

BACKGROUND: Numerous organisms have evolved a wide range of toxic peptides for self-defense and predation. Their effective interstitial and macro-environmental use requires energetic and structural stability. One successful group of these peptides includes a tri-disulfide domain arrangement that offers toxicity and high stability. Sequential tri-disulfide connectivity variants create highly compact disulfide folds capable of withstanding a variety of environmental stresses. Their combination of toxicity and stability make these peptides remarkably valuable for their potential as bio-insecticides, antimicrobial peptides and peptide drug candidates. However, the wide sequence variation, sources and modalities of group members impose serious limitations on our ability to rapidly identify potential members. As a result, there is a need for automated high-throughput member classification approaches that leverage their demonstrated tertiary and functional homology.

Authors

  • S M Ashiqul Islam
    Institute of Biomedical Studies, Baylor University, Waco, TX, USA. S_Islam@Baylor.edu.
  • Tanvir Sajed
    Department of Computer Science, University of Alberta, Edmonton, AB, Canada. Tsajed@ualberta.ca.
  • Christopher Michel Kearney
    Institute of Biomedical Studies, Baylor University, Waco, TX, USA. Chris_Kearney@Baylor.edu.
  • Erich J Baker
    Institute of Biomedical Studies, Baylor University, Waco, TX, USA. Erich_Baker@Baylor.edu.