Requirement of ßDELSEED-Motif of <em>Escherichia coli</em> F₁F_O ATP Synthase in Antimicrobial Peptide Binding.

<p>F₁F_O 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 <em>E. coli</em> 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?</p> <p>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.</p>

Name thesis:degree_name

MS (Master of Science)

Level thesis:degree_level

Thesis - unrestricted

Discipline thesis:degree_discipline

Biology

Year dc:date.issued

2011

Author dc:creator

• Tayou, Junior Kom

• F1FO ATP synthase
• Antimicrobial peptides
• Melittin-NH2 and MRP-NH2 a
• Bacteriology
• Life Sciences
• Microbial Physiology
• Microbiology

Statement dc:rights

• Copyright by the authors.

Repository record dc:identifier

https://dc.etsu.edu/etd/1260

OAI identifier oai:identifier

oai:dc.etsu.edu:etd-2451