title: Identifying therapeutic template by evaluating the structural stability of gram positive anti-bacterial peptides--a computational approach.
abstract: Clinically significant antibiotic resistance has evolved against virtually every antibiotic deployed. Yet the development of new classes of antibiotics has lagged far behind our growing need for such drugs. Antimicrobial peptides (AMPs) have emerged as novel therapeutics hailed for their bactericidal and immunomodulatory properties. However, the process of optimizing antimicrobial peptide stability, using large peptide libraries is both tedious and expensive. The intent of this study is to analyze computationally the stability of anti-bacterial peptides (ABPs), particularly gram positive and to discover a potential template from a pool of ABPs for therapeutic use. Consequently we highlighted that MiAMP1 appears advantageous over the other ABPs with respect to stability, and may provide a convenient platform for the development of anti-bacterial therapeutic peptide.
authors.affiliation: School of Bio Sciences and Technology, Vellore Institute of Technology, Vellore, 632014, Tamil Nadu, India.
authors.forename: K
authors.initials: K
authors.lastname: Ramanathan
authors.forename: Rao
authors.initials: R
authors.lastname: Sethumadhavan
mesh_terms: D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000627:therapeutic use*; D019295:Computational Biology / Q000379:methods*; D030562:Databases, Protein; D006094:Gram-Positive Bacteria / Q000737:chemistry*; D055550:Protein Stability; D013816:Thermodynamics
chemical_list: D023181:Antimicrobial Cationic Peptides