Enhanced metabolic stability and protein-binding properties of artificial α helices derived from a hydrogen-bond surrogate

Application to Bcl-xL

Deyun Wang, Wei Liao, Paramjit Arora

Research output: Contribution to journalArticle

Abstract

(Figure Presented) Artificial á helices prepared by the replacement of a hydrogen bond between residues i and i+4 with a carbon-carbon bond can stabilize biologically relevant peptides in helical conformations (1, internal constraint shaded in gray). α Helices based on hydrogen-bond surrogates that mimic Bak BH3 (2, yellow) can bind their expected protein receptor, Bcl-xL (2, green), with high affinity and resist proteolytic degradation.

Original languageEnglish (US)
Pages (from-to)6525-6529
Number of pages5
JournalAngewandte Chemie - International Edition
Volume44
Issue number40
DOIs
StatePublished - Oct 14 2005

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Hydrogen bonds
Carbon
Conformations
Degradation
Peptides
Proteins
Protein Binding

Keywords

  • Helical structures
  • Hydrogen bonds
  • Molecular recognition
  • Peptidomimetics
  • Protein-protein interactions

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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abstract = "(Figure Presented) Artificial {\'a} helices prepared by the replacement of a hydrogen bond between residues i and i+4 with a carbon-carbon bond can stabilize biologically relevant peptides in helical conformations (1, internal constraint shaded in gray). α Helices based on hydrogen-bond surrogates that mimic Bak BH3 (2, yellow) can bind their expected protein receptor, Bcl-xL (2, green), with high affinity and resist proteolytic degradation.",
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AU - Liao, Wei

AU - Arora, Paramjit

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Y1 - 2005/10/14

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AB - (Figure Presented) Artificial á helices prepared by the replacement of a hydrogen bond between residues i and i+4 with a carbon-carbon bond can stabilize biologically relevant peptides in helical conformations (1, internal constraint shaded in gray). α Helices based on hydrogen-bond surrogates that mimic Bak BH3 (2, yellow) can bind their expected protein receptor, Bcl-xL (2, green), with high affinity and resist proteolytic degradation.

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