Issue 10, 2015

Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologies

Abstract

The HIF-1α/p300 protein–protein interaction plays a key role in tumor metabolism and thus represents a high value target for anticancer drug-development. Although several studies have identified inhibitor candidates using rationale design, more detailed understanding of the interaction and binding interface is necessary to inform development of superior inhibitors. In this work, we report a detailed biophysical analysis of the native interaction with both peptide and Adhiron phage display experiments to identify novel binding motifs and binding regions of the surface of p300 to inform future inhibitor design.

Graphical abstract: Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologies

Supplementary files

Article information

Article type
Paper
Submitted
22 apr 2015
Accepted
08 jun 2015
First published
10 jun 2015
This article is Open Access
Creative Commons BY license

Mol. BioSyst., 2015,11, 2738-2749

Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologies

H. F. Kyle, K. F. Wickson, J. Stott, G. M. Burslem, A. L. Breeze, C. Tiede, D. C. Tomlinson, S. L. Warriner, A. Nelson, A. J. Wilson and T. A. Edwards, Mol. BioSyst., 2015, 11, 2738 DOI: 10.1039/C5MB00284B

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