Computational design of a self-assembling β-peptide oligomer

Ivan V. Korendovych, Yong Ho Kim, Andrew H. Ryan, James D. Lear, William F. Degrado, Scott J. Shandler

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

The first computationally designed self-assembling oligomer consisting of exclusively β-amino acids (βAAs) is presented. The packing of a β-314 helix into coiled-coils of varying stoichiometries as a function of amino acid sequence is examined. β-Peptides with hVal repeating every third residue in the sequence appeared to have a strong propensity to pack into hexameric bundles. The designed sequence was synthesized and characterized with CD spectroscopy, NMR, and analytical ultracentrifugation, suggesting that the peptide adopts a well-folded hexameric structure.

Original languageEnglish (US)
Pages (from-to)5142-5145
Number of pages4
JournalOrganic Letters
Volume12
Issue number22
DOIs
StatePublished - Nov 19 2010

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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    Korendovych, I. V., Kim, Y. H., Ryan, A. H., Lear, J. D., Degrado, W. F., & Shandler, S. J. (2010). Computational design of a self-assembling β-peptide oligomer. Organic Letters, 12(22), 5142-5145. https://doi.org/10.1021/ol102092r