Skip to main content
Kent Academic Repository

Design and Structure of Stapled Peptides Binding to Estrogen Receptors

Phillips, Chris, Roberts, Lee R., Schade, Markus, Bazin, Richard, Bent, Andrew, Davies, Nichola L., Moore, Rob, Pannifer, Andrew D., Pickford, Andrew R., Prior, Stephen H., and others. (2011) Design and Structure of Stapled Peptides Binding to Estrogen Receptors. Journal of the American Chemical Society, 133 (25). pp. 9696-9699. ISSN 0002-7863. (doi:10.1021/ja202946k) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:31351)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1021/ja202946k

Abstract

Synthetic peptides that specifically bind nuclear hormone receptors offer an alternative approach to small molecules for the modulation of receptor signaling and subsequent gene expression. Here we describe the design of a series of novel stapled peptides that bind the coactivator peptide site of estrogen receptors. Using a number of biophysical techniques, including crystal structure analysis of receptor–stapled peptide complexes, we describe in detail the molecular interactions and demonstrate that all-hydrocarbon staples modulate molecular recognition events. The findings have implications for the design of stapled peptides in general.

Item Type: Article
DOI/Identification number: 10.1021/ja202946k
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Susan Davies
Date Deposited: 08 Oct 2012 10:58 UTC
Last Modified: 05 Nov 2024 10:13 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/31351 (The current URI for this page, for reference purposes)

University of Kent Author Information

Brown, David G..

Creator's ORCID:
CReDIT Contributor Roles:
  • Depositors only (login required):

Total unique views for this document in KAR since July 2020. For more details click on the image.