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Publication Abstract from PubMed

The HIF-1alpha/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.

Exploration of the HIF-1alpha/p300 interface using peptide and Adhiron phage display technologies.,Kyle HF, Wickson KF, Stott J, Burslem GM, Breeze AL, Tiede C, Tomlinson DC, Warriner SL, Nelson A, Wilson AJ, Edwards TA Mol Biosyst. 2015 Jul 2. PMID:26135796^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.