Date Approved
8-2013
Date Posted
9-19-2013
Degree Type
Open Access Thesis
Degree Name
Master of Science (MS)
Department or School
Chemistry
Committee Member
Deborah Heyl-Clegg, Ph.D, Chair
Committee Member
Jamie Scaglione, Ph.D., Chair
Committee Member
Hedeel Guy Evans, Ph.D.
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.
Recommended Citation
Srivastava, Mayank, "Chemoenzymatic synthesis of an analogue of the potent antifungal mycosubtilin" (2013). Master's Theses and Doctoral Dissertations. 492.
https://commons.emich.edu/theses/492