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.
| Identifer | oai:union.ndltd.org:ETSU/oai:dc.etsu.edu:etd-2451 |
| Date | 01 May 2011 |
| Creators | Tayou, Junior Kom |
| Publisher | Digital Commons @ East Tennessee State University |
| Source Sets | East Tennessee State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Electronic Theses and Dissertations |
| Rights | Copyright by the authors. |
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