Dr. Richard Payne from the School of Chemistry at The University of Sydney, Australia works on the development of new synthetic methods to facilitate peptide ligation reactions, with a view to their use in the total synthesis of peptides and proteins bearing post-translational modifications. Dr. Payne's laboratory is also interested in the discovery of novel small molecule tuberculosis therapeutics. 

What inspired you to become a scientist? 

My career as a scientist has been shaped by interactions with a number of outstanding mentors. Initial inspiration came from my high school chemistry teacher, who joined the school after many years working as a chemist in industry. His enthusiasm for the subject encouraged me to pursue chemistry at University. I then developed a passion for scientific research through a number of summer research projects in the areas of microbiology, medical biochemistry and organic chemistry during my undergraduate degree at the University of Canterbury (NZ). This early love for science, in particular organic chemistry, was undoubtedly furthered by the time I spent at Cambridge during my PhD (under the supervision of Professor Chris Abell) and my postdoctoral tenure at Scripps (working with Professor Chi-Huey Wong). Having the opportunity to work in two first class departments cemented my desire to pursue a career as an academic. 

What was your motivation behind the work described in your ChemComm article? 

A primary interest of my laboratory is aimed at understanding the biological role of protein glycosylation and phosphorylation. In order to study these biomolecules, one must gain access to them in a homogeneous form. We eventually hope to achieve this goal by synthetic means, specifically by stitching together modified peptide fragments in a convergent manner using peptide ligation chemistry. Although a number of excellent peptide ligation methods already exist, these do not allow direct disconnections at serine and threonine residues. We hope that this can now be realised by the phosphate-assisted peptide ligation methodology reported in our Chemical Communications article. 

Why did you choose ChemComm to publish your work? 

The broad readership and fast publication times were the main reasons for publishing our article in Chemical Communications. We were excited by the results of this study and wanted to disseminate our new methodology to a wide number of researchers as soon as possible. 

Where do you see your research heading next? 

We will continue to develop new ligation methods to facilitate the convergent assembly of post-translationally modified peptides and proteins. These synthetic tools (including our novel phosphate-assisted ligation method) will be implemented in the total synthesis of phosphoproteins and glycoproteins of biological and/or therapeutic significance. The overall goal will be to undertake a detailed structure/function analysis on homogeneous forms of these important biomolecules. 

What do enjoy doing in your spare time? 

Outside of the lab, I enjoy travelling and playing sport, in particular football and cricket. 

If you could not be a scientist, but could be anything else, what would you be? 

A professional footballer! 

Interviewed by Mary Badcock