Towards "bionic" proteins: Replacement of continuous sequences from HIF-1α with proteomimetics to create functional p300 binding HIF-1α mimics

George M. Burslem; Hannah F. Kyle; Alexander L. Breeze; Thomas A. Edwards; Adam Nelson; Stuart L. Warriner; Andrew J. Wilson

doi:10.1039/c6cc01812b

Towards "bionic" proteins: Replacement of continuous sequences from HIF-1α with proteomimetics to create functional p300 binding HIF-1α mimics

George M. Burslem, Hannah F. Kyle, Alexander L. Breeze, Thomas A. Edwards, Adam Nelson, Stuart L. Warriner, Andrew J. Wilson^*

^*Corresponding author for this work

Chemistry

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

17 Citations (Scopus)

Abstract

Using the HIF-1α transcription factor as a model, this manuscript illustrates how an extended sequence of α-amino acids in a polypeptide can be replaced with a non-natural topographical mimic of an α-helix comprised from an aromatic oligoamide. The resultant hybrid is capable of reproducing the molecular recognition profile of the p300 binding sequence of HIF-1α from which it is derived.

Original language	English
Pages (from-to)	5421-5424
Number of pages	4
Journal	Chemical Communications
Volume	52
Issue number	31
DOIs	https://doi.org/10.1039/c6cc01812b
Publication status	Published - 21 Apr 2016

Bibliographical note

Funding Information:
We thank AstraZeneca and EPSRC for PhD studentships (G. M. B. and H. F. K.) and the European Research Council [ERC-StG-240324, and ERC-PoC 632207] for support.

Publisher Copyright:
© The Royal Society of Chemistry 2016.

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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abstract = "Using the HIF-1α transcription factor as a model, this manuscript illustrates how an extended sequence of α-amino acids in a polypeptide can be replaced with a non-natural topographical mimic of an α-helix comprised from an aromatic oligoamide. The resultant hybrid is capable of reproducing the molecular recognition profile of the p300 binding sequence of HIF-1α from which it is derived.",

author = "Burslem, {George M.} and Kyle, {Hannah F.} and Breeze, {Alexander L.} and Edwards, {Thomas A.} and Adam Nelson and Warriner, {Stuart L.} and Wilson, {Andrew J.}",

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doi = "10.1039/c6cc01812b",

language = "English",

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AU - Burslem, George M.

AU - Kyle, Hannah F.

AU - Breeze, Alexander L.

AU - Edwards, Thomas A.

AU - Nelson, Adam

AU - Warriner, Stuart L.

AU - Wilson, Andrew J.

N1 - Funding Information: We thank AstraZeneca and EPSRC for PhD studentships (G. M. B. and H. F. K.) and the European Research Council [ERC-StG-240324, and ERC-PoC 632207] for support. Publisher Copyright: © The Royal Society of Chemistry 2016.

PY - 2016/4/21

Y1 - 2016/4/21

N2 - Using the HIF-1α transcription factor as a model, this manuscript illustrates how an extended sequence of α-amino acids in a polypeptide can be replaced with a non-natural topographical mimic of an α-helix comprised from an aromatic oligoamide. The resultant hybrid is capable of reproducing the molecular recognition profile of the p300 binding sequence of HIF-1α from which it is derived.

AB - Using the HIF-1α transcription factor as a model, this manuscript illustrates how an extended sequence of α-amino acids in a polypeptide can be replaced with a non-natural topographical mimic of an α-helix comprised from an aromatic oligoamide. The resultant hybrid is capable of reproducing the molecular recognition profile of the p300 binding sequence of HIF-1α from which it is derived.

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Towards "bionic" proteins: Replacement of continuous sequences from HIF-1α with proteomimetics to create functional p300 binding HIF-1α mimics

Abstract

Bibliographical note

ASJC Scopus subject areas

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