Reversible α-helix formation controlled by a hydrogen bond surrogate

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...

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Bibliographic Details
Published inTetrahedron Vol. 68; no. 23; pp. 4434 - 4437
Main Authors Miller, Stephen E., Kallenbach, Neville R., Arora, Paramjit S.
Format Journal Article
LanguageEnglish
Published OXFORD Elsevier Ltd 10.06.2012
Elsevier
Subjects
Chemistry
Chemistry, Organic
Disulfide bridge
Foldamer
Helix inducer
Hydrogen bond surrogate
Physical Sciences
Science & Technology
Stabilized α-helix
Stabilized α-helix
Foldamer
Disulfide bridge
Hydrogen bond surrogate
Helix inducer
PEPTIDES
MECHANISM
SOLID-PHASE SYNTHESIS
STABILITY
Stabilized alpha-helix
TRIFLUOROETHANOL
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Summary: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. [Display omitted]
Bibliography:NIH RePORTER
National Science Foundation
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0040-4020
1464-5416
DOI:10.1016/j.tet.2011.12.068