Event Information

Mark Sleeper (Duke University)
The development of tumor-specific enzyme-activated CuII prochelators for use against tumor angiogenesis
Abstract:

Several D-penicillamine and amino-terminal CuII and NiII (ATCUN) binding motif-containing prochelator peptides were synthesized and tested for CuII-binding activity as well as for their ability to be activated via enzymatic cleavage by the cysteine protease Cathepsin B. Of all of the peptides tested against Cathepsin B, Ac-RRGFLG(D-penicillamine)VVWR-NH2 showed the most promise for further investigation due to the large CuII binding differential between its binding-masked prochelator form and the activated chelator (D-penicillamine)VVWR-NH2. In addition, some endoproteolytic cleavage was observed upon exposure to Cathepsin B with this substrate albeit not at the correct peptide bond.

Preliminary Examination Seminar

Monday, April 9, 2012, 1:00pm
Student Exams Seminar