title: PredSTP: a highly accurate SVM based model to predict sequential cystine stabilized peptides.
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.
  
  
  RESULTS
  We developed an SVM-based model to predict sequential tri-disulfide peptide (STP) toxins from peptide sequences. One optimized model, called PredSTP, predicted STPs from training set with sensitivity, specificity, precision, accuracy and a Matthews correlation coefficient of 94.86%, 94.11%, 84.31%, 94.30% and 0.86, respectively, using 200 fold cross validation. The same model outperforms existing prediction approaches in three independent out of sample testsets derived from PDB.
  
  
  CONCLUSIONS
  PredSTP can accurately identify a wide range of cystine stabilized peptide toxins directly from sequences in a species-agnostic fashion. The ability to rapidly filter sequences for potential bioactive peptides can greatly compress the time between peptide identification and testing structural and functional properties for possible antimicrobial and insecticidal candidates. A web interface is freely available to predict STP toxins from http://crick.ecs.baylor.edu/.
authors.affiliation: Institute of Biomedical Studies, Baylor University, Waco, TX, USA. S_Islam@Baylor.edu.
authors.forename: S M Ashiqul
authors.initials: SM
authors.lastname: Islam
authors.affiliation: Department of Computer Science, University of Alberta, Edmonton, AB, Canada. Tsajed@ualberta.ca.
authors.forename: Tanvir
authors.initials: T
authors.lastname: Sajed
authors.affiliation: Institute of Biomedical Studies, Baylor University, Waco, TX, USA. Chris_Kearney@Baylor.edu.|Department of Biology, Baylor University, Waco, TX, USA. Chris_Kearney@Baylor.edu.
authors.forename: Christopher Michel
authors.initials: CM
authors.lastname: Kearney
authors.affiliation: Institute of Biomedical Studies, Baylor University, Waco, TX, USA. Erich_Baker@Baylor.edu.|Department of Computer Science, Baylor University, One Bear Place #97356, Waco, TX, USA. Erich_Baker@Baylor.edu.
authors.forename: Erich J
authors.initials: EJ
authors.lastname: Baker
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D003553:Cystine / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry*; D015233:Models, Statistical; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000494:pharmacology*; D060388:Support Vector Machine
chemical_list: D004220:Disulfides; D010446:Peptide Fragments; D003553:Cystine