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.
","abstract_html":"<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>","abstract_has_math":false,"creators":["Sanders, Karen"],"institution":null,"degree_name":"Master of Science (MS)","degree_level":"Open Access Thesis","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Cory Emal, PhD, Chair","Arthur Howard, PhD","Deborah Heyl-Clegg, PhD"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2010,"date_issued":"2010-01-01T08:00:00Z","date_published":"2010-01-01T08:00:00Z","updated_at":"2026-07-24T02:16:44Z","subjects":["PAI-1","inhibitors","protein inhibitor binding","human ailments","Chemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://commons.emich.edu/theses/370","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Cory Emal, PhD, Chair","Arthur Howard, PhD","Deborah Heyl-Clegg, PhD"]},{"key":"dc:creator","label":"Author","values":["Sanders, Karen"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2012-01-23T08:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Open Access Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science (MS)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["PAI-1","inhibitors","protein inhibitor binding","human ailments","Chemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://commons.emich.edu/theses/370"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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.
"]},{"key":"dc:title","label":"Title","values":["Structure-activity relationships of PAI-1 inhibitors"]}]}],"canonical_facts":{"dc:contributor":["Cory Emal, PhD, Chair","Arthur Howard, PhD","Deborah Heyl-Clegg, PhD"],"dc:creator":["Sanders, Karen"],"dc:date.available":["2012-01-23T08:00:00Z"],"dc:description.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.
"],"dc:identifier":["https://commons.emich.edu/theses/370"],"dc:subject":["PAI-1","inhibitors","protein inhibitor binding","human ailments","Chemistry"],"dc:title":["Structure-activity relationships of PAI-1 inhibitors"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Open Access Thesis"],"thesis:degree_name":["Master of Science (MS)"]},"updated_at":"2026-07-24T02:16:44Z"}