The College of Science proudly congratulates the research team of Asst Prof Liu Xue-Wei and Assoc Prof Liu Chuan-Fa on their joint publication to these top prestigious American Chemical Society publications! This achievement highlights the strength of our joint interdisciplinary research collaboration between the College of Science's School of Physical & Mathematical Sciences (SPMS) and the School of Biological Sciences (SBS).
Front row from left to right: Assoc Prof Liu Chuan-Fa, Asst Prof Liu Xuewei
Back row from left to right: Graduate students Li Fupeng, Yang Renliang and Kalyan Kumar Pasunnooti
Dual Native Chemical Ligation at Lysine
Proteins are the blue-collar molecules of life, charged with the task of doing almost all the biological work in a living organism. The deficiency, overproduction or malfunction of a protein can cause serious diseases such as cancer and metabolic disorders. Therefore the study of how proteins work to exert their functions is a core research area in life science and has attracted the attention of scientists from many disciplines. Chemists tackle the problem by first preparing a protein in bulk and use it to study its structure with biophysical methods and check its biological function in biochemical assays.
In a project founded by a research grant from the A’Star, Assoc Prof Liu Chuan-Fa’s lab at SBS worked together with Asst Prof Liu Xuewei’s lab at SPMS to develop a new method for the chemical synthesis of proteins. Their work is in press in an upcoming issue of The Journal of the American Chemical Society (the web version was published on September 3, 2009). Highlighting the importance of their work, Chemical & Engineering News – a weekly chemistry news magazine published by the American Chemical Society – featured a Concentrate news item about their new method in the September 21, 2009 issue.
The method developed by the team offers significant advantage over existing technology in the preparation of large and complex protein molecules containing specially modified lysine amino acid. As such their work provides a useful tool not only for the functional elucidation of protein post-translational modification in basic biology but also for the development of protein-based therapeutics in medicine.
Link to JACS paper (requires NTU subscription)
J. Am. Chem. Soc., Articles ASAP (As Soon As Publishable);
Publication Date (Web): September 3, 2009 (Communication)
Link to C&EN news (requires NTU subscription)
Chemical & Engineering News, Science & Technology Concentrates, September 21, 2009, Volume 87, Number 38 p. 35
Abstract:
A thiol group introduced on the gamma-carbon of lysine mediates robust native chemical ligation at both the alpha- and epsilon-amines in two consecutive steps. Desulfurization then affords the final product, in which the lysine residue at the ligation site has an isopeptide bond on its side chain. The method is useful for the synthesis of proteins containing special post-translational modifications on lysine.