Reversible α-helix formation controlled by a hydrogen bond surrogate

Stephen E. Miller, Neville R. Kallenbach, Paramjit Arora

Research output: Contribution to journalArticle

Abstract

Strategically placed covalent linkages have been shown to stabilize helical conformations in short peptide sequences. Here we report the synthesis of a stabilized α-helix that utilizes an internal disulfide linkage. Structural analysis indicates that the dynamic nature of the disulfide bridge allows for the reversible formation of an α-helix through oxidation and reduction reactions.

Original languageEnglish (US)
Pages (from-to)4434-4437
Number of pages4
JournalTetrahedron
Volume68
Issue number23
DOIs
StatePublished - Jun 10 2012

Fingerprint

Disulfides
Hydrogen
Hydrogen bonds
Structural analysis
Oxidation-Reduction
Conformations
Oxidation
Peptides

Keywords

  • Disulfide bridge
  • Foldamer
  • Helix inducer
  • Hydrogen bond surrogate
  • Stabilized α-helix

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry
  • Drug Discovery

Cite this

Reversible α-helix formation controlled by a hydrogen bond surrogate. / Miller, Stephen E.; Kallenbach, Neville R.; Arora, Paramjit.

In: Tetrahedron, Vol. 68, No. 23, 10.06.2012, p. 4434-4437.

Research output: Contribution to journalArticle

Miller, Stephen E. ; Kallenbach, Neville R. ; Arora, Paramjit. / Reversible α-helix formation controlled by a hydrogen bond surrogate. In: Tetrahedron. 2012 ; Vol. 68, No. 23. pp. 4434-4437.
@article{b466c274566c496f955fe44176c19c9f,
title = "Reversible α-helix formation controlled by a hydrogen bond surrogate",
abstract = "Strategically placed covalent linkages have been shown to stabilize helical conformations in short peptide sequences. Here we report the synthesis of a stabilized α-helix that utilizes an internal disulfide linkage. Structural analysis indicates that the dynamic nature of the disulfide bridge allows for the reversible formation of an α-helix through oxidation and reduction reactions.",
keywords = "Disulfide bridge, Foldamer, Helix inducer, Hydrogen bond surrogate, Stabilized α-helix",
author = "Miller, {Stephen E.} and Kallenbach, {Neville R.} and Paramjit Arora",
year = "2012",
month = "6",
day = "10",
doi = "10.1016/j.tet.2011.12.068",
language = "English (US)",
volume = "68",
pages = "4434--4437",
journal = "Tetrahedron",
issn = "0040-4020",
publisher = "Elsevier Limited",
number = "23",

}

TY - JOUR

T1 - Reversible α-helix formation controlled by a hydrogen bond surrogate

AU - Miller, Stephen E.

AU - Kallenbach, Neville R.

AU - Arora, Paramjit

PY - 2012/6/10

Y1 - 2012/6/10

N2 - Strategically placed covalent linkages have been shown to stabilize helical conformations in short peptide sequences. Here we report the synthesis of a stabilized α-helix that utilizes an internal disulfide linkage. Structural analysis indicates that the dynamic nature of the disulfide bridge allows for the reversible formation of an α-helix through oxidation and reduction reactions.

AB - Strategically placed covalent linkages have been shown to stabilize helical conformations in short peptide sequences. Here we report the synthesis of a stabilized α-helix that utilizes an internal disulfide linkage. Structural analysis indicates that the dynamic nature of the disulfide bridge allows for the reversible formation of an α-helix through oxidation and reduction reactions.

KW - Disulfide bridge

KW - Foldamer

KW - Helix inducer

KW - Hydrogen bond surrogate

KW - Stabilized α-helix

UR - http://www.scopus.com/inward/record.url?scp=84860659333&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84860659333&partnerID=8YFLogxK

U2 - 10.1016/j.tet.2011.12.068

DO - 10.1016/j.tet.2011.12.068

M3 - Article

AN - SCOPUS:84860659333

VL - 68

SP - 4434

EP - 4437

JO - Tetrahedron

JF - Tetrahedron

SN - 0040-4020

IS - 23

ER -