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Dr Joel D A Tyndall
National School of Pharmacy
University of Otago
PO Box 913 Dunedin
Email: joel.tyndall@otago.ac.nz
Tel: +64-3-4797293
Fax: +64-3-4797034

Research focuses on characteristics of protease recognition of ligands.
This encompasses the relationships between their structural folds,
catalytic mechanism, recognition of substrates and other ligands and
notable correlations between classes and subclasses. This has borne out
the premise that proteases recognise substrates and inhibitors in an
extended peptide conformation with almost no exceptions. The design of
inhibitors has been successful against HIV-1 protease and on going
research is being conducted into the protein modelling and inhibitor
design of flaviviral NS3 proteases of Dengue fever and West Nile virus.
Similar efforts are targeting the parasitic Schistosomal cathepsin with
an aim to developing selective and potent inhibitors. Recent isolation
and characterisation of a novel protease from a cone snail has
identified the function of a protein with significant homology with the
pathogenesis-related protein superfamily.
Professor David Fairlie University of Queensland, Australia
Dr Willa Huston, Queensland University of Technology, Australia
Dr Michael Kelso, University of Wollongong, Australia
Dr Marie Ranson, University of Wollongong, Australia
Milne, T.J., Abbenante, G., Tyndall, J.D.A., Halliday, J., Lewis, R.J.,
Isolation and characterization of a cone snail protease with homology
to CRISP proteins of the pathogenesis-related protein superfamily. J.
Biol. Chem, 2003, 278(33), p31105-10.
Tyndall, J.D.A. and Fairlie, D.P., Macrocycles mimic the extended
peptide conformation recognized by aspartic, serine, cysteine and
metallo proteases. Curr Med Chem, 2001. 8(8): p. 893-907.
Tyndall, J.D.A., Reid, R.C., Tyssen, D.P., Jardine, D.K., Todd, B.,
Passmore, M., March, D.R., Pattenden, L.K., Bergman, D.A., Alewood, D.,
Hu, S.H., Alewood, P.F., Birch, C.J., Martin, J.L., and Fairlie, D.P.,
Synthesis, stability, antiviral activity, and protease-bound structures
of substrate-mimicking constrained macrocyclic inhibitors of HIV-1
protease. J Med Chem, 2000. 43(19): p. 3495-504.
Fairlie, D.P., Tyndall, J.D.A., Reid, R.C., Wong, A.K., Abbenante, G.,
Scanlon, M.J., March, D.R., Bergman, D.A., Chai, C.L., and Burkett,
B.A., Conformational selection of inhibitors and substrates by
proteolytic enzymes: implications for drug design and polypeptide
processing. J Med Chem, 2000. 43(7): p. 1271-81.
Tyndall, J.D.A. and Fairlie, D.P., Conformational homogeneity in
molecular recognition by proteolytic enzymes. J Mol Recognit, 1999.
12(6): p. 363-70.

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