Date of Award


Degree Type


Degree Name

Master of Science




Dr. Leonard G. Luyt


Receptor for hyaluronan mediated motility (Rhamm), is a extracellular receptor for hyaluronan, which is over-expressed in breast cancer. To develop imaging probes for Rhamm, peptide mimics of hyaluronan (HA) were developed using: (1) screening of combinatorial peptide library, and (2) basic local alignment search tool (BLAST) to elucidate proteins high affinity ligands. Using combinatorial approach, a library consisting of D-peptides was screened and resulted in 15 novel peptides showing micromolar affinities. Through rational-based approach, 17 tubulin-derived peptides were screening using surface plasmon spectroscopy (SPR) and resulted in 6 high affinity ligands with nanomolar affinities. Using enzyme-linked immunosorbent assay (ELISA), candidate peptides from the two approaches showed specificity to the Rhamm's HA binding domain and were able to compete with HA for binding. Rhenium (I) complexes containing the/oc-M(CO)3+moieties served as surrogates forfac- 99mTc(CO)3+ complexes, which are fundamental in the development of radioactive products for diagnostic applications. Rhenium tricarbonyl complexes incorporating bi- and tridentate bis(l-methylbenzimidazol-2-yl) ligands were developed, synthesized and characterized spectroscopically.



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