Professor Philip Hogg, Director, Lowy Cancer Research Centre, The University of New South Wales.
Protein action in nature is largely controlled by the amount of protein made and by chemical modifications. Once proteins are made by cells they are chemically modified in a variety of ways to control where, when and for how long they function. Posttranslational modifications of amino acid side chains and the peptide bonds that link amino acids have been well characterised.
A third fundamental type of posttranslational modification has recently been identified that involves the disulphide bonds that bind the polypeptide backbone. The features of this modification and what the future holds for this field of research will be discussed.
Professor Philip Hogg is a biochemist and directs the Lowy Cancer Research Centre on the University of New South Wales campus in Sydney. All life forms make proteins that contain strong bonds between pairs of cysteine amino acids called disulphide bonds. Phil and his team have shown that some disulphide bonds have evolved to control how mature proteins work by breaking or forming in a precise way. He has called these bonds 'allosteric' disulphides. Application of this basic research has led to the development of two novel anti-cancer drugs that are both in clinical testing.