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The molecular basis of interfacial recognition by human secreted phospholipase A2

Reference	C11772
Principal Investigator / Supervisor	Dr D Wilton
Co-Investigators / Co-Supervisors
Institution	University of Southampton
Department	Centre for Biological Sciences
Funding type	Research
Value (£)	167,768
Status	Completed
Type	Research Grant
Start date	01/05/2000
End date	30/04/2003
Duration	36 months

Abstract

Secreted phospholipases A are a model for the study of molecular interactions involved in interfacial binding and catalysis. Human sPLA2 is of special interest as it is released as part of the bodies response to infection and trauma. The enzyme is essentially inactive against neutral phosphatidyl choline vesicles and normal cell membranes in contrast to the structurally very similar snake venom and pancreatic enzymes. Using a unique E. coli expression system and site directed mutagenesis we will determine why this human enzyme does not hydrolyse neutral host cell membranes. We will mutate residues that make up the hydrophobic collar within the interfacial binding surface of the enzyme in order to understand how these hydrophobic residues contribute to interfacial binding and cell membrane hydrolysis. A specific objective is to engineer a fluorescent interfacial probe to detect anionic interfaces and for interfacial binding assays.

Summary

unavailable

Committee	Closed Committee - Biochemistry & Cell Biology (BCB)
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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