Imperial College London
Alternate

Professor Karen Polizzi

Faculty of Engineering, Department of Chemical Engineering

Professor of Biotechnology
 
 
 
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Contact

 

+44 (0)20 7594 2851k.polizzi

 
 
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Location

 

411ACE ExtensionSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Arpino:2020:10.1021/acssynbio.9b00504,
author = {Arpino, JAJ and Polizzi, KM},
doi = {10.1021/acssynbio.9b00504},
journal = {ACS Synthetic Biology},
pages = {993--1002},
title = {A modular method for directing protein self-assembly},
url = {http://dx.doi.org/10.1021/acssynbio.9b00504},
volume = {9},
year = {2020}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Proteins are versatile macromolecules with diverse structure, charge, and function. They are ideal building blocks for biomaterials for drug delivery, biosensing, or tissue engineering applications. Simultaneously, the need to develop green alternatives to chemical processes has led to renewed interest in multienzyme biocatalytic routes to fine, specialty, and commodity chemicals. Therefore, a method to reliably assemble protein complexes using protein-protein interactions would facilitate the rapid production of new materials. Here we show a method for modular assembly of protein materials using a supercharged protein as a scaffolding "hub" onto which target proteins bearing oppositely charged domains have been self-assembled. The physical properties of the material can be tuned through blending and heating and disassembly triggered using changes in pH or salt concentration. The system can be extended to the synthesis of living materials. Our modular method can be used to reliably direct the self-assembly of proteins using small charged tag domains that can be easily encoded in a fusion protein.
AU  - Arpino,JAJ
AU  - Polizzi,KM
DO  - 10.1021/acssynbio.9b00504
EP  - 1002
PY  - 2020///
SN  - 2161-5063
SP  - 993
TI  - A modular method for directing protein self-assembly
T2  - ACS Synthetic Biology
UR  - http://dx.doi.org/10.1021/acssynbio.9b00504
UR  - https://www.ncbi.nlm.nih.gov/pubmed/32243747
UR  - https://pubs.acs.org/doi/10.1021/acssynbio.9b00504
UR  - http://hdl.handle.net/10044/1/78080
VL  - 9
ER  -
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