Antimicrobial peptides act against bacteria by binding non-specifically and disrupting their outer membrane. LL-37 is the only member of the cathelicidin group of antimicrobial peptides present in humans and shows a broad range of antimicrobial activity. RK-21 is a fragment of human antimicrobial peptide LL-37, which is α-helical, cationic and amphipathic in nature. RK-21 displays similar antimicrobial activity to LL- 37. In order to understand the mechanism of lipid bilayer disruption, fluorine-labeled antimicrobial peptide RK-21 was chemically synthesized and 19F-NMR studies were done. NMR studies were done at various peptide concentrations, on different lipid bilayer compositions and temperatures. 31P-NMR studies did not show any micellar fragments, eliminating the detergent-like mechanism for activity. 19F-NMR studies indicated that labeled RK-21 is oriented on glass stack lipid samples. The peptide maintained this orientation at different lipid compositions, different peptide concentrations and different temperatures. Preliminary results support a mechanism of toroidal pore formation. iv
","abstract_html":"<p>Antimicrobial peptides act against bacteria by binding non-specifically and disrupting their outer membrane. LL-37 is the only member of the cathelicidin group of antimicrobial peptides present in humans and shows a broad range of antimicrobial activity. RK-21 is a fragment of human antimicrobial peptide LL-37, which is α-helical, cationic and amphipathic in nature. RK-21 displays similar antimicrobial activity to LL- 37. In order to understand the mechanism of lipid bilayer disruption, fluorine-labeled antimicrobial peptide RK-21 was chemically synthesized and 19F-NMR studies were done. NMR studies were done at various peptide concentrations, on different lipid bilayer compositions and temperatures. 31P-NMR studies did not show any micellar fragments, eliminating the detergent-like mechanism for activity. 19F-NMR studies indicated that labeled RK-21 is oriented on glass stack lipid samples. The peptide maintained this orientation at different lipid compositions, different peptide concentrations and different temperatures. Preliminary results support a mechanism of toroidal pore formation. iv</p>","abstract_has_math":false,"creators":["Budarapu, Mahender"],"institution":null,"degree_name":"Master of Science (MS)","degree_level":"Open Access Thesis","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2007,"date_issued":"2007-01-01T08:00:00Z","date_published":"2007-01-01T08:00:00Z","updated_at":"2026-07-24T02:16:24Z","subjects":["Peptide antibiotics analysis","Chemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://commons.emich.edu/theses/18","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Budarapu, Mahender"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Open Access Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science (MS)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Peptide antibiotics analysis","Chemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://commons.emich.edu/theses/18"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Antimicrobial peptides act against bacteria by binding non-specifically and disrupting their outer membrane. LL-37 is the only member of the cathelicidin group of antimicrobial peptides present in humans and shows a broad range of antimicrobial activity. RK-21 is a fragment of human antimicrobial peptide LL-37, which is α-helical, cationic and amphipathic in nature. RK-21 displays similar antimicrobial activity to LL- 37. In order to understand the mechanism of lipid bilayer disruption, fluorine-labeled antimicrobial peptide RK-21 was chemically synthesized and 19F-NMR studies were done. NMR studies were done at various peptide concentrations, on different lipid bilayer compositions and temperatures. 31P-NMR studies did not show any micellar fragments, eliminating the detergent-like mechanism for activity. 19F-NMR studies indicated that labeled RK-21 is oriented on glass stack lipid samples. The peptide maintained this orientation at different lipid compositions, different peptide concentrations and different temperatures. Preliminary results support a mechanism of toroidal pore formation. iv
"]},{"key":"dc:title","label":"Title","values":["Synthesis and solid state F-NMR studies on fluorine-labeled antimicrobial peptide RK-21"]}]}],"canonical_facts":{"dc:creator":["Budarapu, Mahender"],"dc:description.abstract":["Antimicrobial peptides act against bacteria by binding non-specifically and disrupting their outer membrane. LL-37 is the only member of the cathelicidin group of antimicrobial peptides present in humans and shows a broad range of antimicrobial activity. RK-21 is a fragment of human antimicrobial peptide LL-37, which is α-helical, cationic and amphipathic in nature. RK-21 displays similar antimicrobial activity to LL- 37. In order to understand the mechanism of lipid bilayer disruption, fluorine-labeled antimicrobial peptide RK-21 was chemically synthesized and 19F-NMR studies were done. NMR studies were done at various peptide concentrations, on different lipid bilayer compositions and temperatures. 31P-NMR studies did not show any micellar fragments, eliminating the detergent-like mechanism for activity. 19F-NMR studies indicated that labeled RK-21 is oriented on glass stack lipid samples. The peptide maintained this orientation at different lipid compositions, different peptide concentrations and different temperatures. Preliminary results support a mechanism of toroidal pore formation. iv
"],"dc:identifier":["https://commons.emich.edu/theses/18"],"dc:subject":["Peptide antibiotics analysis","Chemistry"],"dc:title":["Synthesis and solid state F-NMR studies on fluorine-labeled antimicrobial peptide RK-21"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Open Access Thesis"],"thesis:degree_name":["Master of Science (MS)"]},"updated_at":"2026-07-24T02:16:24Z"}