{"id":{"repo_id":"utmb","oai_identifier":"oai:utmb-ir.tdl.org:2152.3/215"},"canonical_url":"https://search.dev.ndltd.org/etd/utmb/oai:utmb-ir.tdl.org:2152.3/215","repository":{"repo_id":"utmb","name":"University of Texas Medical Branch","base_url":"https://utmb-ir.tdl.org/server/oai/request"},"display":{"title":"Solid phase peptide synthesis and TLR-5 activity analysis of pertide fragments from the Salmonella muenchen flagellin protein","abstract":"Drug design strategies begin by determining the simplest ligand necessary to activate a receptor of interest. The Toll-Like Receptor-5 (TLR-5) is an attractive target for pharmaceutical modulation because it initiates an innate immune response. A TLR-5 agonist or antagonist could help remedy a variety of disorders. Flagellin, the primary component of bacterial flagella, is the only known TLR-5 ligand. Three short regions within this protein are suggested to activate TLR-5: Peptide-N1, LQRVRELAVQ; Peptide-N2, LAVQSANGTNSQSD; and Peptide-C1, QNRFNSAITNLGNT. Here, we report the synthesis of these peptides and their activity against TLR-5 expressing HEK-293 cells. Our goal was to resolve the minimal region of flagellin necessary to bind and/or activate TLR-5. Results showed significant agonist activity (P<0.01) with peptide N2-b (LAVQSANGTN), and peptide N2-f (LAVQSANGTNSQ). Peptide N2-c (ANGTN) and N2-d (LAVQS) showed significant (P<0.05) antagonistic properties for TLR-5. These peptides could make interesting lead compounds to modify for optimal TLR-5 activity.","abstract_html":"Drug design strategies begin by determining the simplest ligand necessary to activate a receptor of interest. The Toll-Like Receptor-5 (TLR-5) is an attractive target for pharmaceutical modulation because it initiates an innate immune response. A TLR-5 agonist or antagonist could help remedy a variety of disorders. Flagellin, the primary component of bacterial flagella, is the only known TLR-5 ligand. Three short regions within this protein are suggested to activate TLR-5: Peptide-N1, LQRVRELAVQ; Peptide-N2, LAVQSANGTNSQSD; and Peptide-C1, QNRFNSAITNLGNT. Here, we report the synthesis of these peptides and their activity against TLR-5 expressing HEK-293 cells. Our goal was to resolve the minimal region of flagellin necessary to bind and/or activate TLR-5. Results showed significant agonist activity (P<0.01) with peptide N2-b (LAVQSANGTN), and peptide N2-f (LAVQSANGTNSQ). Peptide N2-c (ANGTN) and N2-d (LAVQS) showed significant (P<0.05) antagonistic properties for TLR-5. These peptides could make interesting lead compounds to modify for optimal TLR-5 activity.","abstract_has_math":false,"creators":["Joseph Richard Karam"],"institution":"The University of Texas Medical Branch","degree_name":"Master of Science","degree_level":"Master","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Dr. Scott R. Gilbertson, Ph.D."],"committee_chairs":[],"committee_members":["Dr. Richard B. Pyles, Ph.D","Dr. Cornelis Elfernik, Ph.D."],"year":2005,"date_issued":"2005-08-18","date_published":"2005-08-18","updated_at":"2026-07-24T05:51:09Z","subjects":["toll-like receptor","innate immunity","drug synthesis and design"],"languages":["eng"],"rights":["Copyright © is held by the author. Presentation of this material on the TDL web site by The University of Texas Medical Branch at Galveston was made possible under a limited license grant from the author who has retained all copyrights in the works."],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["etd-08222005-204822"],"render_values":[{"text":"etd-08222005-204822","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2152.3/215","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Dr. Scott R. Gilbertson, Ph.D."]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Dr. Richard B. 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Three short regions within this protein are suggested to activate TLR-5: Peptide-N1, LQRVRELAVQ; Peptide-N2, LAVQSANGTNSQSD; and Peptide-C1, QNRFNSAITNLGNT. Here, we report the synthesis of these peptides and their activity against TLR-5 expressing HEK-293 cells. Our goal was to resolve the minimal region of flagellin necessary to bind and/or activate TLR-5. Results showed significant agonist activity (P<0.01) with peptide N2-b (LAVQSANGTN), and peptide N2-f (LAVQSANGTNSQ). Peptide N2-c (ANGTN) and N2-d (LAVQS) showed significant (P<0.05) antagonistic properties for TLR-5. These peptides could make interesting lead compounds to modify for optimal TLR-5 activity."]},{"key":"dc:format.medium","label":"Dc Format Medium","values":["electronic"]},{"key":"dc:title","label":"Title","values":["Solid phase peptide synthesis and TLR-5 activity analysis of pertide fragments from the Salmonella muenchen flagellin protein"]}]}],"canonical_facts":{"dc:contributor.advisor":["Dr. Scott R. 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