Award details

Evolving proteins complementary to nanopatterned surfaces

Reference	E15786
Principal Investigator / Supervisor	Professor Wilhelm Huck
Co-Investigators / Co-Supervisors	Dr Paul Barker
Institution	University of Cambridge
Department	Chemistry
Funding type	Research
Value (£)	214,504
Status	Completed
Type	Research Grant
Start date	11/03/2002
End date	25/04/2005
Duration	37 months

Abstract

Biomolecules that self-assemble into defined arrangements upon patterned, nanometer size, solid state structures will be important in nanotechnology. This project will engineer both protein surfaces and solid state surfaces as a means of providing perfect complementarity between them. This will facilitate the positioning of useful functional proteins in a defined and stable manner. Based on protein scaffolds already shown to bind to solid crystal lattices, the type III antifreeze proteins, we will use a rationally random approach to find protein variants that bind with high affinity, or covalently, to solid state surfaces, such as silicon oxide, and lattices generated via microcontact printing of functionalised SAMs. We will begin to pattern SAMs down to molecular dimensions in order to study adhesion of single proteins. In short we will be combining nanolithographical and molecular biological technologies.

Summary

unavailable

Committee	Closed Committee - Engineering & Biological Systems (EBS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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