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

25 Citations (Scopus)

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

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Dichroism
Circular Dichroism
helices
dichroism
bundles
peptides
signatures
Peptides
assembling
Self assembly
self assembly
Screening
screening
assembly

Cite this

Distinctive circular dichroism signature for 14-helix-bundle formation by ß-peptides. / Pomerantz, William C.; Grygiel, Tami L R; Lai, Jonathan R.; Gellman, Samuel H.

In: Organic Letters, Vol. 10, No. 9, 01.05.2008, p. 1799-1802.

Research output: Contribution to journalArticle

Pomerantz, William C. ; Grygiel, Tami L R ; Lai, Jonathan R. ; Gellman, Samuel H. / Distinctive circular dichroism signature for 14-helix-bundle formation by ß-peptides. In: Organic Letters. 2008 ; Vol. 10, No. 9. pp. 1799-1802.
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