@-tides as reporters for molecular associations

Scott T. Phillips, Landy K. Blasdel, Paul A. Bartlett

Research output: Contribution to journalArticle

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Abstract

The 1,6-dihydro-3(2H)-pyridinone unit is an amino acid surrogate that favors the extended α-strand conformation when incorporated in an oligopeptide ("@-tide") strand. We now report that the circular dichroism (CD) signature of the vinylogous amide in the @-unit is sensitive to conformation in organic and aqueous solvents and, therefore, is useful as a quantitative measure of @-tide association and folding processes that involve this moiety. Moreover, this method can be employed in the micromolar concentration range, which is not readily accessible using other techniques. Measurements of @-tide dimerization and β-hairpin folding equilibria not only demonstrate the utility and generality of this approach but also provide a way to quantify amino acid side chain-side chain interactions relevant to β-sheet stability.

Original languageEnglish (US)
Pages (from-to)4193-4198
Number of pages6
JournalJournal of the American Chemical Society
Volume127
Issue number12
DOIs
Publication statusPublished - Mar 30 2005

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All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Phillips, S. T., Blasdel, L. K., & Bartlett, P. A. (2005). @-tides as reporters for molecular associations. Journal of the American Chemical Society, 127(12), 4193-4198. https://doi.org/10.1021/ja045122w