Award details

Chemical and structural integrity of proteins in the glassy state

Reference	BB/C504600/1
Principal Investigator / Supervisor	Professor Christopher Smales
Co-Investigators / Co-Supervisors	Dr Mark Howard
Institution	University of Kent
Department	Sch of Biosciences
Funding type	Research
Value (£)	185,285
Status	Completed
Type	Research Grant
Start date	28/02/2005
End date	27/08/2008
Duration	42 months

Abstract

The aim of this programme of work is to determine the physical and chemical basis and mechanisms of globular protein stability in the glassy state. From empirically-developed industrial practices, two strategies for achieving stability using glassy states can be identified and from these two hypotheses developed. The first concerns the minimisation of molecular mobility in glassy matrices and the second the additional use of specific interactions in protein-polyelectrolyte complexes to achieve stability. To tackle this multi- and cross-disciplinary problem requires expertise in protein chemistry and the physical chemistry of biopolymer glasses. Model proteins have been selected for tractable mass spectrometry (ms) and NMR structural analyses. In order to characterise the chemistry and consequent structural modifications, the reactions of peptides with structural context will be used and their reactions in the glassy state screened using ms and circular dichroism. Molecular mobility in glasses will be characterised through calorimetric measurements of glass transition temperatures and structural relaxation rates and electron paramagnetic resonance (EPR) spin label and probe studies of local and global mobility. NMR structural analysis will be performed on the modification to model peptides and proteins. The conditions under which polyelectrolyte complexation occurs will be characterised and its consequent effect on probe mobility and chemical stability. The overall goal is a model relating chemical and physical stability of proteins to the glassy state. While some aspects of the programme will investigate the type of chemical reactions which can proceed in the glass, there will also be detailed kinetic studies of how glassy matrices affect the reaction at the peptide level (chemical reaction) and protein level (aggregation). (Joint with BB/C504478/1).

Summary

unavailable

Committee	Closed Committee - Agri-food (AF)
Research Topics	Structural Biology
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

Associated awards:

BB/C504478/1 Chemical and structural integrity of proteins in the glassy state

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