Degree Name
MS (Master of Science)
Program
Biology
Date of Award
8-2023
Committee Chair or Co-Chairs
Dr. Valentin Yakubenko
Committee Members
Dr. Dhirendra Kumar, Dr. Patrick Bradshaw
Abstract
Neutrophils and macrophages accumulate at sites of inflammation and cause chronic inflammation leading to various diseases. Therefore, to better understand chronic disease pathways it is important to investigate the properties of macrophage accumulation in inflamed tissues. The I-domain of the macrophage receptor integrin aDb2 plays a vital role in macrophage retention by binding to CEP (carboxyethyl pyrrole), a ligand available at inflammatory sites. This thesis mainly focuses on evaluating the binding site within integrin aDb2 that binds carboxyethyl pyrrole (CEP)-modified proteins. So, a recombinant plasmid construct containing the integrin I-domain was developed. Seven non-conserved amino acids were mutated by PCR-site-directed mutagenesis to create a mutant construct. After expressing in E. coli, the binding affinities of wild-type and mutant I-domains to CEP were analyzed using biolayer interferometry. It was found that a patch of seven positively charged amino acids contributes to the strong binding of the I domain to CEP.
Document Type
Thesis - embargo
Recommended Citation
Prema, Afia, "Mapping The Binding Site Within Integrin D2 for Carboxyethylpyrrole (CEP)-Modified Proteins" (2023). Electronic Theses and Dissertations. Paper 4232. https://dc.etsu.edu/etd/4232
Copyright
Copyright by the authors.