Environment- and Sequence-dependence of Helical Type in Membrane-spanning Peptides Composed of β3-amino Acids

Overview

Journal Org Lett

Publisher American Chemical Society

Specialties Biochemistry
Chemistry

Date 2011 Jun 10

PMID 21651308

Citations 4

Authors

Ivan V Korendovych

Scott J Shandler

Geronda L Montalvo

William F DeGrado

Affiliations

Soon will be listed here.

Abstract

Transmembrane (TM) β-peptides comprised of acyclic β(3)-amino acids demonstrate equilibrium between 12- and 14-helical structures in an environment- and sequence-dependent manner. Circular dichroism (CD) spectra of TM β(3)-peptides may be described as linear combinations of the 12- and 14-helical CD spectra. The apparent malleability of β(3)-substituted acyclic β-peptides has practical implications for foldamer design, as it suggests that both the 14-helix and 12-helix might be reasonable platforms for molecular recognition.

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