Exploration of structural features of monomeric helical peptides designed with a genetic algorithm

Wuming Zhang, Micheal G. Loughran, Shin Ichi Kanna, Kazuyoshi Yano, Kazunori Ikebukuro, Yohei Yokobayashi, Reiko Kuroda, Isao Karube

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

A genetic algorithm (GA)-based strategy to dissect the determinants of peptide folding into α-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 α-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 α-helix content.

Original languageEnglish (US)
Pages (from-to)193-200
Number of pages8
JournalProteins: Structure, Function and Genetics
Volume53
Issue number2
DOIs
StatePublished - Nov 1 2003
Externally publishedYes

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Keywords

  • Alpha-helix
  • Circular dichroism
  • De novo design
  • Electrostatic interactions
  • Evolution
  • Networks
  • Protein folding
  • Salt bridges
  • Side-chain interactions

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

Zhang, W., Loughran, M. G., Kanna, S. I., Yano, K., Ikebukuro, K., Yokobayashi, Y., Kuroda, R., & Karube, I. (2003). Exploration of structural features of monomeric helical peptides designed with a genetic algorithm. Proteins: Structure, Function and Genetics, 53(2), 193-200. https://doi.org/10.1002/prot.10509