Nucleation and stability of hydrogen-bond surrogate-based α-helices

Deyun Wang, Kang Chen, Gianluca Dimartino, Paramjit S. Arora

Research output: Contribution to journalArticle

Abstract

We have reported a new class of artificial α-helices in which a pre-organized α-turn nucleates the helical conformation [R. N. Chapman, G. Dimartino, and P. S. Arora, J. Am. Chem. Soc., 2004, 126, 12252 and D. Wang, K. Chen, J. L. Kulp, III, and P. S. Arora, J. Am. Chem. Soc., 2006, 128, 9248]. This manuscript describes the effect of the core nucleation template on the overall helicity of the peptides and demonstrates that the macrocycle which most closely mimics the 13-membered hydrogen-bonded α-turn in canonical α-helices also affords the most stable artificial α-helix. We also investigate the stability of these synthetic helices through classical helix-coil parameters and find that the denaturation behavior of HBS α-helices agrees with the theoretical properties of a peptide with a well-defined and stable helix nucleus.

Original languageEnglish (US)
Pages (from-to)4074-4081
Number of pages8
JournalOrganic and Biomolecular Chemistry
Volume4
Issue number22
DOIs
StatePublished - 2006

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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