Exploration of structural features of monomeric helical peptides designed with a genetic algorithm.
A genetic algorithm (GA)-based strategy to dissect the determinants of peptide folding into alpha-helix was developed. The structural information of helical peptides was obtained with respect to patterns of sequence variability. In many previously reported studies the intrinsic alpha-helical propensities of amino acids although sequence-dependent are apparently independent of the amino acid position. In this research, monomeric helical peptides selected from possible sequences produced by a GA-chemical synthesis were analyzed to identify possible influential structural features. These hexadeca-peptides were obtained after four successive generations. A total of 128 synthetic peptides were evaluated via circular dichroism (CD) measurements in aqueous solution, while the mean ellipticity at 222 nm confirmed the monomeric state of the peptides. The results presented here show that our GA-based strategy may be useful in the design of proteins with increased alpha-helix content.
D000465:Algorithms; D002942:Circular Dichroism; D008957:Models, Genetic; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000235:genetics; D017354:Point Mutation; D017433:Protein Structure, Secondary
D010455:Peptides