Helix nucleation by the smallest known α-helix in water

Hoang, Huy N., Driver, Russell W., Beyer, Renee L., Hill, Timothy A., de Araujo, Aline D., Plisson, Fabien, Harrison, Rosemary S., Goedecke, Lena, Shepherd, Nicholas E. and Fairlie, David P. (2016) Helix nucleation by the smallest known α-helix in water. Angewandte Chemie (International Edition), 55 29: 8275-8279. doi:10.1002/anie.201602079

Author Hoang, Huy N.
Driver, Russell W.
Beyer, Renee L.
Hill, Timothy A.
de Araujo, Aline D.
Plisson, Fabien
Harrison, Rosemary S.
Goedecke, Lena
Shepherd, Nicholas E.
Fairlie, David P.
Title Helix nucleation by the smallest known α-helix in water
Journal name Angewandte Chemie (International Edition)   Check publisher's open access policy
ISSN 1521-3773
Publication date 2016-07-11
Year available 2016
Sub-type Letter to editor, brief commentary or brief communication
DOI 10.1002/anie.201602079
Open Access Status Not yet assessed
Volume 55
Issue 29
Start page 8275
End page 8279
Total pages 5
Place of publication Weinheim, Germany
Publisher Wiley - V C H Verlag GmbH & Co. KGaA
Collection year 2017
Language eng
Formatted abstract
Cyclic pentapeptides (e.g. Ac-(cyclo-1,5)-[KAXAD]-NH2; X=Ala, 1; Arg, 2) in water adopt one α-helical turn defined by three hydrogen bonds. NMR structure analysis reveals a slight distortion from α-helicity at the C-terminal aspartate caused by torsional restraints imposed by the K(i)–D(i+4) lactam bridge. To investigate this effect on helix nucleation, the more water-soluble 2 was appended to N-, C-, or both termini of a palindromic peptide ARAARAARA (≤5 % helicity), resulting in 67, 92, or 100 % relative α-helicity, as calculated from CD spectra. From the C-terminus of peptides, 2 can nucleate at least six α-helical turns. From the N-terminus, imperfect alignment of the Asp5 backbone amide in 2 reduces helix nucleation, but is corrected by a second unit of 2 separated by 0–9 residues from the first. These cyclic peptides are extremely versatile helix nucleators that can be placed anywhere in 5–25 residue peptides, which correspond to most helix lengths in protein–protein interactions.
Keyword Circular dichroism
Cyclic peptides
Helical structures
Helix nucleation
NMR spectroscopy
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Letter to editor, brief commentary or brief communication
Collections: HERDC Pre-Audit
Institute for Molecular Bioscience - Publications
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 1 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 1 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 28 Jun 2016, 02:22:22 EST by System User on behalf of Learning and Research Services (UQ Library)