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

Hannah F. Kyle; Kate F. Wickson; Jonathan Stott; George M. Burslem; Alexander L. Breeze; Christian Tiede; Darren C. Tomlinson; Stuart L. Warriner; Adam Nelson; Andrew J. Wilson; Thomas A. Edwards

doi:10.1039/c5mb00284b

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

Hannah F. Kyle, Kate F. Wickson, Jonathan Stott, George M. Burslem, Alexander L. Breeze, Christian Tiede, Darren C. Tomlinson, Stuart L. Warriner, Adam Nelson, Andrew J. Wilson, Thomas A. Edwards^*

^*Corresponding author for this work

Chemistry

Research output: Contribution to journal › Article › peer-review

30 Citations (Scopus)

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.

Original language	English
Pages (from-to)	2738-2749
Number of pages	12
Journal	Molecular BioSystems
Volume	11
Issue number	10
DOIs	https://doi.org/10.1039/c5mb00284b
Publication status	Published - 8 Jun 2015

Bibliographical note

Publisher Copyright:
© The Royal Society of Chemistry 2015.

ASJC Scopus subject areas

Biotechnology
Molecular Biology

Access to Document

10.1039/c5mb00284b

Cite this

@article{fa1de8832de249d1a8b1b5da15d8ddac,

title = "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.",

author = "Kyle, {Hannah F.} and Wickson, {Kate F.} and Jonathan Stott and Burslem, {George M.} and Breeze, {Alexander L.} and Christian Tiede and Tomlinson, {Darren C.} and Warriner, {Stuart L.} and Adam Nelson and Wilson, {Andrew J.} and Edwards, {Thomas A.}",

note = "Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2015.",

year = "2015",

month = jun,

day = "8",

doi = "10.1039/c5mb00284b",

language = "English",

volume = "11",

pages = "2738--2749",

journal = "Molecular BioSystems",

issn = "1742-206X",

publisher = "Royal Society of Chemistry",

number = "10",

}

TY - JOUR

T1 - Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologies

AU - Kyle, Hannah F.

AU - Wickson, Kate F.

AU - Stott, Jonathan

AU - Burslem, George M.

AU - Breeze, Alexander L.

AU - Tiede, Christian

AU - Tomlinson, Darren C.

AU - Warriner, Stuart L.

AU - Nelson, Adam

AU - Wilson, Andrew J.

AU - Edwards, Thomas A.

PY - 2015/6/8

Y1 - 2015/6/8

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84941801317&partnerID=8YFLogxK

U2 - 10.1039/c5mb00284b

DO - 10.1039/c5mb00284b

M3 - Article

C2 - 26135796

AN - SCOPUS:84941801317

SN - 1742-206X

VL - 11

SP - 2738

EP - 2749

JO - Molecular BioSystems

JF - Molecular BioSystems

IS - 10

ER -

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

Abstract

Bibliographical note

ASJC Scopus subject areas

Access to Document

Fingerprint

Cite this