Structure-activity relationships of PAI-1 inhibitors

<p>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.</p>

Name thesis:degree_name

Master of Science (MS)

Level thesis:degree_level

Open Access Thesis

Discipline thesis:degree_discipline

Chemistry

Year dc:date.available

2010

Author dc:creator

• Sanders, Karen

Contributors dc:contributor

• Cory Emal, PhD, Chair
• Arthur Howard, PhD
• Deborah Heyl-Clegg, PhD

• PAI-1
• inhibitors
• protein inhibitor binding
• human ailments
• Chemistry

Repository record dc:identifier

https://commons.emich.edu/theses/370

OAI identifier oai:identifier

oai:commons.emich.edu:theses-1370