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Katzenellenbogen, John A. Fink, Brian Edward 2015-09-25T22:14:17Z 2015-09-25T22:14:17Z 10000-01-01 1998 1998 We have prepared novel aspartic proteases inhibitors based on the diaziridine and diazirine isostere, as potential transition-state mimics of the tetrahedral intermediate found along the reaction pathway for enzyme mediated peptide bond hydrolysis. These isosteres (143 and 144) have been incorporated into substrates for the aspartic protease pepsin, however they did not show any inhibition. Made available in DSpace on 2015-09-25T22:14:17Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9834673.pdf: 8586536 bytes, checksum: 9a272136bcff46118789def3420acce2 (MD5) Previous issue date: 1998 Embargo set by: Seth Robbins for item 85677 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 184 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1998. http://hdl.handle.net/2142/84396 (MiAaPQ)AAI9834673 eng Biology, Animal Physiology I.~Design, Synthesis, and Evaluation of a Rigidly Constrained Peptidomimetic as a Potential Type I Beta-Turn. II.~Development of Novel Estrogen Receptor Ligands With Unique Endocrine Profiles. III.~Design, Synthesis and Biological Evaluation of Potential Aspartic Protease Inhibitors Based on the Diaziridine and Diazirine Isostere text Chemistry Chemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.