Date Approved
2010
Degree Type
Open Access Thesis
Degree Name
Master of Science (MS)
Department or School
Chemistry
Committee Member
Cory Emal, PhD, Chair
Committee Member
Arthur Howard, PhD
Committee Member
Deborah Heyl-Clegg, PhD
Abstract
The inhibition of plasminogen activator inhibitor-1 (PAI-1) is anticipated to increase our understanding of various human ailments with which high levels of PAI-1 have been associated, including diabetes, stroke, and atherosclerosis. Previous accounts have reported the synthesis of inhibitors that bind to PAI-1 with a low affinity, inhibit the serpin plasma protein antithrombin III, and/or fail to inhibit PAI-1 when vitronectin, a cofactor of PAI-1 is present. The synthesis of small-molecule inhibitors of PAI-1 that improve upon these properties has been the main goal of this research. Research efforts focused on examining changes in inhibitor potency based on the manipulation of the inhibitors’ architecture, with particular attention paid to the number and positioning of multiple polyphenolic groups. The refinement of these synthesized moieties into selective and highly active species has been achieved.
Recommended Citation
Sanders, Karen, "Structure-activity relationships of PAI-1 inhibitors" (2010). Master's Theses and Doctoral Dissertations. 370.
https://commons.emich.edu/theses/370