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NMR solution structure of a photoswitchable apoptosis activating Bak peptide bound to Bcl-xL

Wysoczanski, Piotr, Mart, Robert J., Loveridge, Edric Joel, Williams, Christopher, Whittaker, Sara B.-M., Crump, Matthew P. and Allemann, Rudolf Konrad 2012. NMR solution structure of a photoswitchable apoptosis activating Bak peptide bound to Bcl-xL. Journal of the American Chemical Society 134 (18) , pp. 7644-7647. 10.1021/ja302390a

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Abstract

The Bcl-2 family of proteins includes the major regulators and effectors of the intrinsic apoptosis pathway. Cancers are frequently formed when activation of the apoptosis mechanism is compromised either by misregulated expression of prosurvival family members or, more frequently, by damage to the regulatory pathways that trigger intrinsic apoptosis. Short peptides derived from the pro-apoptotic members of the Bcl-2 family can activate mechanisms that ultimately lead to cell death. The recent development of photocontrolled peptides that are able to change their conformation and activity upon irradiation with an external light source has provided new tools to target cells for apoptosis induction with temporal and spatial control. Here, we report the first NMR solution structure of a photoswitchable peptide derived from the proapoptotic protein Bak in complex with the antiapoptotic protein Bcl-xL. This structure provides insight into the molecular mechanism, by which the increased affinity of such photopeptides compared to their native forms is achieved, and offers a rationale for the large differences in the binding affinities between the helical and nonhelical states.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Cardiff Catalysis Institute (CCI)
Chemistry
Subjects: Q Science > QD Chemistry
Publisher: American Chemical Society
ISSN: 1520-5126
Funders: EPSRC, Wellcome Trust
Last Modified: 09 Sep 2019 22:59
URI: http://orca.cf.ac.uk/id/eprint/35089

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