Mycosubtilin is a naturally occurring antifungal obtained from Bacillus subtilis that also displays limited antibiotic activity. Structurally, mycosubtilin is a macrocycliclipoheptapeptide of sequence Asn-Tyr-Asn-Gln-Pro-Ser-Asn, with the N-terminal Asn joined by a β-amino fatty acid. Besides the antifungal and antibiotic activities,these molecules are also hemolytic in nature. Hence, the purpose of this study is to synthesize a potent antifungal analogue of mycosubtilin, with a modified β-amino fatty acid, devoid of any hemolytic activity. A chemoenzymatic approach was used to synthesize the cyclic peptide, which involved the synthesis of the linear peptide chain of desired amino acid sequence, thiophenylderivatization of the peptide at the C-terminus, followed by its enzymatic cyclization using the isolated thioesterase from B. subtilis. Thus far, we have successfully synthesized the analogue of mycosubtilin. Future work will focus on purifying the product and testing it for antifungal and hemolytic activity.
","abstract_html":"<p>Mycosubtilin is a naturally occurring antifungal obtained from <em>Bacillus subtilis</em> that also displays limited antibiotic activity. Structurally, mycosubtilin is a macrocycliclipoheptapeptide of sequence Asn-Tyr-Asn-Gln-Pro-Ser-Asn, with the N-terminal Asn joined by a β-amino fatty acid. Besides the antifungal and antibiotic activities,these molecules are also hemolytic in nature. Hence, the purpose of this study is to synthesize a potent antifungal analogue of mycosubtilin, with a modified β-amino fatty acid, devoid of any hemolytic activity. A chemoenzymatic approach was used to synthesize the cyclic peptide, which involved the synthesis of the linear peptide chain of desired amino acid sequence, thiophenylderivatization of the peptide at the C-terminus, followed by its enzymatic cyclization using the isolated thioesterase from <em>B. subtilis</em>. Thus far, we have successfully synthesized the analogue of mycosubtilin. Future work will focus on purifying the product and testing it for antifungal and hemolytic activity.</p>","abstract_has_math":false,"creators":["Srivastava, Mayank"],"institution":null,"degree_name":"Master of Science (MS)","degree_level":"Open Access Thesis","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Deborah Heyl-Clegg, Ph.D, Chair","Jamie Scaglione, Ph.D., Chair","Hedeel Guy Evans, Ph.D."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2013,"date_issued":"2013-08-01T07:00:00Z","date_published":"2013-08-01T07:00:00Z","updated_at":"2026-07-24T02:16:51Z","subjects":["bacillus subtilis","antibiotics","molecules","Organic Chemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://commons.emich.edu/theses/492","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Deborah Heyl-Clegg, Ph.D, Chair","Jamie Scaglione, Ph.D., Chair","Hedeel Guy Evans, Ph.D."]},{"key":"dc:creator","label":"Author","values":["Srivastava, Mayank"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2013-09-16T07:00:00Z"]},{"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":["bacillus subtilis","antibiotics","molecules","Organic Chemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://commons.emich.edu/theses/492"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Mycosubtilin is a naturally occurring antifungal obtained from Bacillus subtilis that also displays limited antibiotic activity. Structurally, mycosubtilin is a macrocycliclipoheptapeptide of sequence Asn-Tyr-Asn-Gln-Pro-Ser-Asn, with the N-terminal Asn joined by a β-amino fatty acid. Besides the antifungal and antibiotic activities,these molecules are also hemolytic in nature. Hence, the purpose of this study is to synthesize a potent antifungal analogue of mycosubtilin, with a modified β-amino fatty acid, devoid of any hemolytic activity. A chemoenzymatic approach was used to synthesize the cyclic peptide, which involved the synthesis of the linear peptide chain of desired amino acid sequence, thiophenylderivatization of the peptide at the C-terminus, followed by its enzymatic cyclization using the isolated thioesterase from B. subtilis. Thus far, we have successfully synthesized the analogue of mycosubtilin. Future work will focus on purifying the product and testing it for antifungal and hemolytic activity.
"]},{"key":"dc:title","label":"Title","values":["Chemoenzymatic synthesis of an analogue of the potent antifungal mycosubtilin"]}]}],"canonical_facts":{"dc:contributor":["Deborah Heyl-Clegg, Ph.D, Chair","Jamie Scaglione, Ph.D., Chair","Hedeel Guy Evans, Ph.D."],"dc:creator":["Srivastava, Mayank"],"dc:date.available":["2013-09-16T07:00:00Z"],"dc:description.abstract":["Mycosubtilin is a naturally occurring antifungal obtained from Bacillus subtilis that also displays limited antibiotic activity. Structurally, mycosubtilin is a macrocycliclipoheptapeptide of sequence Asn-Tyr-Asn-Gln-Pro-Ser-Asn, with the N-terminal Asn joined by a β-amino fatty acid. Besides the antifungal and antibiotic activities,these molecules are also hemolytic in nature. Hence, the purpose of this study is to synthesize a potent antifungal analogue of mycosubtilin, with a modified β-amino fatty acid, devoid of any hemolytic activity. A chemoenzymatic approach was used to synthesize the cyclic peptide, which involved the synthesis of the linear peptide chain of desired amino acid sequence, thiophenylderivatization of the peptide at the C-terminus, followed by its enzymatic cyclization using the isolated thioesterase from B. subtilis. Thus far, we have successfully synthesized the analogue of mycosubtilin. Future work will focus on purifying the product and testing it for antifungal and hemolytic activity.
"],"dc:identifier":["https://commons.emich.edu/theses/492"],"dc:subject":["bacillus subtilis","antibiotics","molecules","Organic Chemistry"],"dc:title":["Chemoenzymatic synthesis of an analogue of the potent antifungal mycosubtilin"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Open Access Thesis"],"thesis:degree_name":["Master of Science (MS)"]},"updated_at":"2026-07-24T02:16:51Z"}