Department or Program

Biological Chemistry


Tissue Plasminogen Activator (tPA) is a protein associated with endothelial fibrinolysis and is implicated as a potential biomarker for several disorders including multiple cancers, as well as neurovascular, inflammatory, and renal conditions. Through a process of selective evolution of ligands by exponential enrichment (SELEX), RNA aptamers were isolated to specifically bind the tPA protein. RNA aptamers developed were sequenced, and secondary structures determined to compare to an aptamer previously described. It was determined that products of our SELEX procedure underwent a significant deletion that abolished binding in both the control aptamer and random template. Our results indicate that the template design and SELEX process were ineffective at isolating a tPA-binding aptamer, and further work is needed to avoid the deletion product. Further research of the conformational structure of the RNA sites recognized by tPA may improve our understanding of its role in a number of cellular signaling pathways and its ability, as a potential biomarker, to predict prognostic information concerning several associated medical conditions.

Level of Access

Restricted: Embargoed [Bates Community After Expiration]

First Advisor

Schlax, Paula

Date of Graduation


Degree Name

Bachelor of Science

Number of Pages


Components of Thesis

1 pdf file


Available to Bates Community via local IP address or Bates login on Tuesday, May 01, 2029.