{"id":{"repo_id":"etsu","oai_identifier":"oai:dc.etsu.edu:etd-2451"},"canonical_url":"https://search.dev.ndltd.org/etd/etsu/oai:dc.etsu.edu:etd-2451","repository":{"repo_id":"etsu","name":"East Tennessee State University","base_url":"https://dc.etsu.edu/do/oai/"},"display":{"title":"Requirement of ßDELSEED-Motif of <em>Escherichia coli</em> F<sub>1</sub>F<sub>O</sub> ATP Synthase in Antimicrobial Peptide Binding.","abstract":"<p>F<sub>1</sub>F<sub>O</sub> 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>","abstract_html":"&lt;p&gt;F&lt;sub&gt;1&lt;/sub&gt;F&lt;sub&gt;O&lt;/sub&gt; 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 &lt;em&gt;E. coli&lt;/em&gt; 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?&lt;/p&gt; &lt;p&gt;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.&lt;/p&gt;","abstract_has_math":false,"creators":["Tayou, Junior Kom"],"institution":null,"degree_name":"MS (Master of Science)","degree_level":"Thesis - unrestricted","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-01T07:00:00Z","date_published":"2011-05-01T07:00:00Z","updated_at":"2026-07-24T02:20:06Z","subjects":["F1FO ATP synthase","Antimicrobial peptides","Melittin-NH2 and MRP-NH2 a","Bacteriology","Life Sciences","Microbial Physiology","Microbiology"],"languages":[],"rights":["Copyright by the authors."],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://dc.etsu.edu/etd/1260","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Tayou, Junior Kom"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["1990-01-01T08:00:00Z"]},{"key":"dc:date.issued","label":"Date","values":["2011-05-01T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis - unrestricted"]},{"key":"thesis:degree_name","label":"Degree Name","values":["MS (Master of Science)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["F1FO ATP synthase","Antimicrobial peptides","Melittin-NH2 and MRP-NH2 a","Bacteriology","Life Sciences","Microbial Physiology","Microbiology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["Copyright by the authors."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://dc.etsu.edu/context/etd/article/2451/viewcontent/TayouJ041511f.pdf","https://dc.etsu.edu/etd/1260"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["<p>F<sub>1</sub>F<sub>O</sub> 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>"]},{"key":"dc:title","label":"Title","values":["Requirement of ßDELSEED-Motif of <em>Escherichia coli</em> F<sub>1</sub>F<sub>O</sub> ATP Synthase in Antimicrobial Peptide Binding."]}]}],"canonical_facts":{"dc:creator":["Tayou, Junior Kom"],"dc:date.available":["1990-01-01T08:00:00Z"],"dc:date.issued":["2011-05-01T07:00:00Z"],"dc:description.abstract":["<p>F<sub>1</sub>F<sub>O</sub> 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>"],"dc:identifier":["https://dc.etsu.edu/context/etd/article/2451/viewcontent/TayouJ041511f.pdf","https://dc.etsu.edu/etd/1260"],"dc:rights":["Copyright by the authors."],"dc:subject":["F1FO ATP synthase","Antimicrobial peptides","Melittin-NH2 and MRP-NH2 a","Bacteriology","Life Sciences","Microbial Physiology","Microbiology"],"dc:title":["Requirement of ßDELSEED-Motif of <em>Escherichia coli</em> F<sub>1</sub>F<sub>O</sub> ATP Synthase in Antimicrobial Peptide Binding."],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Thesis - unrestricted"],"thesis:degree_name":["MS (Master of Science)"]},"updated_at":"2026-07-24T02:20:06Z"}