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Issue 10, 2015
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Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologies

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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

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Publication details

The article was received on 22 apr. 2015, accepted on 08 jún. 2015 and first published on 10 jún. 2015


Article type: Paper
DOI: 10.1039/C5MB00284B
Citation: Mol. BioSyst., 2015,11, 2738-2749
  • Open access: Creative Commons BY license
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    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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