Dr Steven Cobb
(email at firstname.lastname@example.org)
Steven Cobb carried out his PhD with Professor David O’Hagan at St. Andrews University (2001-2005). His work focused on the biosynthesis of fluorinated natural products, in the bacteria Streptomyces cattleya. The highlight of this research was the identification of the first ever naturally-occurring C-F bond forming enzyme (Nature, 2002, 416, 279). Steven was awarded an Alberta Heritage Foundation for Medical Research Fellowship and moved to the University of Alberta, to work with Professor John Vederas, FRS. During this time he was introduced to the field of peptide chemistry and he worked on the development of new peptide based antibiotics. In October 2007 Steven moved to the Chemistry Department at Durham University as a temporary lecturer, and from this position he was awarded a prestigious Ramsay Memorial Trust Research Fellowship (2008–2010). In 2010 he was appointed to the position of Lecturer and since then he has attracted research funding from various competitive sources as a PI including the Royal Society, the EPSRC, The Wellcome Trust, The Leverhulme Trust, UK industry and he was recently the successful PI on a Bill and Melinda Gates Foundation Grant (one of only 100 grants award worldwide from over 2100 applications).
Our group uses a range of methods and techniques in synthetic organic and peptide chemistry to tackle interesting and challenging biological problems.
Some project highlights include:
New antiparasitics inspired by naturally occurring antimicrobial peptides are being developed in collaboration with researchers both at Durham (Dr Paul Denny) and at the Walter Reed Army Institute of Medical Research (Maryland, US).
Working with Dr Ehmke Pohl (Durham, Protein Crystallography) and Professors Simi Ali and John Kirby (Newcastle University, Medical School) peptide inhibitors of chemokine induced chemotaxis are being designed, with the aim of reducing inflammation and thus protecting cardiac tissue during heart by-pass operations.
New biomaterials and light activated peptide drug delivery systems that exploit novel amino acids prepared in the group are being developed in collaboration with Dr Karl Coleman (Durham) and Dr Ka-La Wong (Hong Kong Baptist University) respectively.
Utilising Solid Phase Peptide Synthesis (SPPS) novel amino acids probes prepared within the group are being incorporated site specifically in small proteins (up to 200 amino acids in size). The incorporation of these novel amino acids provides a reactive handle for selective and controlled protein modification or they enable information about a specific protein to be gathered using a range of biophysical techniques. At the present time we are carrying out the total chemical synthesis of several targets with the aim of providing labelled proteins that can be used as to understand things such as protein-protein interactions and protein misfolding in a range of diseases.
For further details, see my personal web pages
Department of Chemistry
- Biological Chemistry
- Peptide Drug Design and Delivery
- Bioorganic Fluorine Chemistry
Journal papers: academic
- Saleki, M, Colgin, N, Kirby, JA, Cobb, SL & Ali, S (2013). Evaluation of two cyclic di-peptides as inhibitors of CCL2 induced chemotaxis. MedChemComm 4(5): 860-864.