The peptide under initial investigation is hemokinin (HK1), a decapeptide member of the tachykinin family of peptides identified in the mouse with the sequence SRTRQFYGLM-NH2. The equivalent human peptides are termed “endokinins” and differ in a number of subtle ways from hemokinin. The biology of the peptides is not well understood, although it is believed they play an important part in the regulation of the circulatory system. The approach will be twofold involving both organic synthesis and molecular biology. (i) Synthesis of hemokinin analogues will be carried out in proof of concept studies using a novel general ligation strategy developed in the Harwood group that does away with the need for a cysteine residue at the N-terminus, and permits Fmoc protection for generating the C–terminus thioester. (ii) Binding to mouse tachykinin receptors will be studind using radiolabelled HK1 analogues to establish structure activity profiles and identify agonists/antagonists. The analogues will also be studied for their role in platelet function – specifically secretion, integrin affinity modulation and aggregation, and through studying the cell signalling generated by these and the cell lines, develop an understanding of which specific receptors are of importance for the responses observed. These studies mesh with current expertise and interests with the Bicknell and Gibbins groups and might be further extended to endokinin analogues. Applications forms are available from Mrs. Judy Butler, Postgraduate Secretary, Chemistry Department, University of Reading, Whiteknights, Reading, Berks, RG6 6AD, Telephone Number: 01183786591 or by email j.m.butler@reading.ac.uk. Application Deadline October2010 Read more: http://scholarship-positions.com/phd-studentshipsynthetic-and-structure-activity-studies-on-hemokinin-and-analoguesuniversity-of-reading-uk/2010/08/10/?utm_source=feedburner&utm_medium=feed&utm_campaign=Feed%3A+ScholarshipPositions+%28International+Scholarships+and+Financial+Aid+Positions%29&utm_content=Yahoo%21+Mail#ixzz0x8foh5VQ