Date Approved
3-15-2014
Degree Type
Open Access Thesis
Degree Name
Master of Science (MS)
Department or School
Chemistry
Committee Member
Cory Emal, PhD, Chair
Committee Member
Gregg Wilmes, PhD
Committee Member
Steven Pernecky, PhD
Abstract
Plasminogen activator inhibitor-1 (PAI-1) is a member of the serpin family of proteins, a primary inhibitor of both tissue-type and urokinase-type plasminogen activators in plasma, and is a well-established risk factor in various disease conditions. Increased levels of active PAI-1 in plasma are correlated with the development of atherosclerosis, diabetes, stroke, and other maladies. In the present study, we describe the synthesis of two new series of compounds that aim to reduce physiologically active PAI-1 levels. These molecules are related to a series of bis-arylsulfonimides and arylsulfonamides connected by short linking diamines, and to a series of hydrazine-based analogues. These studies resulted in the identification of small molecule inhibitors of PAI-1 that displayed in vitro IC50 values in the low micromolar range.
Recommended Citation
Anumala, Himabindu, "Design, synthesis, and biological evaluation of non-symmetric smal" (2014). Master's Theses and Doctoral Dissertations. 701.
https://commons.emich.edu/theses/701