Distinctive circular dichroism signature for 14-helix-bundle formation by ß-peptides

William C. Pomerantz, Tami L.R. Grygiel, Jonathan R. Lai, Samuel H. Gellman

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

We identify a distinctive circular dichroism (CD) signature for self-assembled 14-helical ß-peptides. Our data show that self-assembly leads to a mimimum at 205 nm, which is distinct from the well-known minimum at 214 nm for a monomeric 14-helix. The onset of assembly is indicated by [θ]205/[θ]214 > 0.7. Our results will facilitate rapid screening for self-assembling ß-peptides and raise the possibility that far-UV CD will be useful for detecting higher-order structure for other well-folded oligoamide backbones.

Original languageEnglish (US)
Pages (from-to)1799-1802
Number of pages4
JournalOrganic Letters
Volume10
Issue number9
DOIs
StatePublished - May 1 2008
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Distinctive circular dichroism signature for 14-helix-bundle formation by ß-peptides'. Together they form a unique fingerprint.

  • Cite this