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Requirement Of Ssdelseed-Motif Of Escherichia Coli F1FO Atp Synthase In Antimicrobial Peptide Binding., Junior Kom Tayou
Requirement Of Ssdelseed-Motif Of Escherichia Coli F1FO Atp Synthase In Antimicrobial Peptide Binding., Junior Kom Tayou
Electronic Theses and Dissertations
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 …