MS (Master of Science)
Date of Award
Committee Chair or Co-Chairs
Michael S. Zavada
Thomas F. Laughlin, Dhirena Kumar
F1FO ATP synthase is a membrane bound enzyme capable of synthesizing and hydrolyzing ATP. Lately, α-helical cationic peptides such as melittin and melittin related peptide (MRP) were shown to inhibit E. coli ATP synthase. The proposed but unconfirmed site of inhibition is βDELSEED-motif formed by the residues 380-386, located at the interface of α/β subunit of ATP synthase. This project was a mutagenic analysis of βDELSEED-motif residues to understand the binding mechanism and mode of action of peptide inhibitors. The study addressed 2 main questions: Are the antibacterial/anticancer effects of these peptides related to their inhibitory action on ATP synthase through interaction with the βDELSEED-motif? If so, which amino acid residues play critical role in peptide binding?
The findings demonstrated that the βDELSEED-motif is the binding site of the above peptides on ATP synthase and Glutamate residues are more important in peptide binding than the Aspartate residues.
Thesis - Open Access
Tayou, Junior Kom, "Requirement of ßDELSEED-Motif of Escherichia coli F1FO ATP Synthase in Antimicrobial Peptide Binding." (2011). Electronic Theses and Dissertations. Paper 1260. http://dc.etsu.edu/etd/1260
Copyright by the authors.