RESEARCH IN THIS LABORATORY IS ON CHEMISTRY AND BIOLOGY OF PEPTIDES.
Chemistry: This laboratory is well-equipped to carry out
synthesis of a wide variety of peptides by the solid phase
method. Improvements in synthetic methods are being
developed. J.M. Stewart was the designer of the first
instrument for automatic peptide synthesis and collaborated
with R.B. Merrifield on development of the solid-phase
method, for which Merrifield won the Nobel prize. The
Stewart laboratory has carried out syntheses of a wide
variety of peptides during more than 3 decades of
research.
Biology: Current research deals with the following
interests: Development of more potent bradykinin antagonists
and application of them to the pathophysiology of
inflammation and cancer. Physiological roles of the
neuropeptide Substance P and elucidation of new SP receptors
in the central nervous system. Analogs of luteinizing
hormone releasing hormone, opioid peptides, scorpion venom
peptides. Study of the rules governing protein folding and
the design and synthesis of new enzymes.
Representative Publications:
Bradykinin antagonists: Present progress and future
prospects. J.M. Stewart, L. Gera, E.J. York, D.C. Chan and
P. Bunn. Immunopharmacology 43: 155-161, 1999.
Novel bradykinin antagonist dimers for the treatment of
human lung cancers. D. Chan, L. Gera, B. Helfrich, K. Helm,
J. Stewart, E. Whalley and P. Bunn. Immunopharmacology 33:
201-204, 1996.
Potent, long-acting, orally-active bradykinin antagonists
for a wide range of applications. J.M. Stewart, L. Gera,
D.C. Chan, E.T. Whalley, W.L. Hanson and J.S. Zuzack.
Immunopharmacology 36: 167-172, 1997.
NMR and CD conformational studies of bradykinin and its
agonists and antagonists: Application to receptor binding.
G. Kotovych, J.R. Cann, J.M.Stewart and H. Yamamoto.
Biochem. Cell Biol. 76: 257-266, 1998.
Neuropeptide processing in pathophysiology. J.M. Stewart
and M.E. Hall. Agents and Actions 42S: 211-226, 1993.
Studies on chymotrypsin-like catalysis by synthetic
peptides. M.J. Corey,. Hallakova, K. Pugh and J.M. Stewart.
App. Biochem. Biotechnol., 47:199-212, 1994.
Helix propensities of basic amino acids increase with the
length of the side-chain. S. Padmanabhan, E.J. York, J.M.
Stewart and R.L. Baldwin. J. Mol. Biol. 257: 726-734, 1996.
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