Reversible α-helix formation controlled by a hydrogen bond surrogate

Stephen E. Miller; Neville R. Kallenbach; Paramjit S. Arora

doi:10.1016/j.tet.2011.12.068

Reversible α-helix formation controlled by a hydrogen bond surrogate

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

Chemistry

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	4434-4437
Number of pages	4
Journal	Tetrahedron
Volume	68
Issue number	23
DOIs	https://doi.org/10.1016/j.tet.2011.12.068
State	Published - Jun 10 2012

Keywords

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

ASJC Scopus subject areas

Biochemistry
Drug Discovery
Organic Chemistry

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10.1016/j.tet.2011.12.068

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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 Arora, {Paramjit S.}",

note = "Funding Information: This work was financially supported by the National Science Foundation ( CHE1027009 to N.R.K.) and the National Institutes of Health ( GM073943 to P.S.A.). S.E.M. thanks the New York University Department of Chemistry for a Margaret Strauss Kramer Predoctoral Fellowship. Support from the National Science Foundation ( CHE-0958457 ) in the form of an instrumentation grant is gratefully acknowledged. ",

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

AU - Miller, Stephen E.

AU - Kallenbach, Neville R.

AU - Arora, Paramjit S.

N1 - Funding Information: This work was financially supported by the National Science Foundation ( CHE1027009 to N.R.K.) and the National Institutes of Health ( GM073943 to P.S.A.). S.E.M. thanks the New York University Department of Chemistry for a Margaret Strauss Kramer Predoctoral Fellowship. Support from the National Science Foundation ( CHE-0958457 ) in the form of an instrumentation grant is gratefully acknowledged.

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

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JO - Tetrahedron

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Reversible α-helix formation controlled by a hydrogen bond surrogate

Abstract

Keywords

ASJC Scopus subject areas

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