To give a flavour of the work carried out in my group, the
following pages provide a simplified summary of a recent piece of research
to use combinatorial peptide libraries in order to select tight-binding
inhibitors of serine proteases. Full details can be found in the following
|McBride, J.D., Freeman, N., Domingo, G.J. and Leatherbarrow, R.J.
(1996) Selection of chymotrypsin inhibitors from a conformationally-constrained
combinatorial library. J. Mol. Biol. 259, 819-827.
Aims of this Research
Protease inhibitors have great potential therapeutic importance, and many
such inhibitors are used in the pharmaceutical industry. Their applications
include anti-coagulants, anti-inflammatory and anti-viral agents. There is
great interest both in development of new inhibitors of this class, and in
understanding the basic processes of protease inhibition. This present work,
which is funded by GlaxoSmithKline, had the following immediate aims: