{"id":51,"date":"2012-10-24T16:01:29","date_gmt":"2012-10-24T16:01:29","guid":{"rendered":"http:\/\/blogs.kent.ac.uk\/biosciences\/?p=51"},"modified":"2012-10-24T16:20:41","modified_gmt":"2012-10-24T16:20:41","slug":"structural-insights-into-targets-for-tumour-imaging-and-therapy","status":"publish","type":"post","link":"https:\/\/blogs.kent.ac.uk\/biosciences\/2012\/10\/24\/structural-insights-into-targets-for-tumour-imaging-and-therapy\/","title":{"rendered":"Structural insights into targets for tumour imaging and therapy"},"content":{"rendered":"

Dr. Mark Howard<\/a>, Reader in Biological NMR Spectroscopy, comments on a recently published article that features work from his research group and other collaborators at Kent and elsewhere.<\/p>\n

“Our research involves nuclear magnetic resonance spectroscopy, a scientific method that can determine the shape and flexibility of molecules.\u00a0 The molecules we studied in this paper were peptides that are known to bind to a cell surface molecule, integrin avb6, a known cancer marker and of medical interest as a target for tumour imaging and therapy. This paper points to important molecular features in these peptides that make them specific toward the integrin and so useful for medical applications.\u00a0 This study is part of an ongoing collaboration with John Marshall\u2019s group at the Barts Institute of Cancer, London.”<\/p>\n

\"Integrin<\/a><\/p>\n

Dr. Howard is\u00a0a key member of our teaching team,\u00a0introducing the importance of chemistry in biology and bringing his expertise to teaching the structure and function of proteins.<\/p>\n

NMR relaxation and structural elucidation of peptides in the presence and absence of trifluoroethanol illuminates the critical molecular nature of integrin a<\/strong>vb<\/strong>6 ligand specificity. Jane L. Wagstaff, Michelle L. Rowe, Shu-Ju Hsieh, Danielle DiCara, John F. Marshall, Richard A. Williamson and Mark J. Howard. <\/strong>RSC Advances, 2012, 2<\/strong>, 11019\u201311028.<\/a><\/p>\n