[HTML][HTML] Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologies
HF Kyle, KF Wickson, J Stott, GM Burslem… - Molecular …, 2015 - pubs.rsc.org
Molecular BioSystems, 2015•pubs.rsc.org
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 …
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 …
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.
The Royal Society of Chemistry