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JOURNAL ARTICLE
RESEARCH SUPPORT, N.I.H., EXTRAMURAL
RESEARCH SUPPORT, NON-U.S. GOV'T
Structure-Activity Relationships of the S-Linked Glycocin Sublancin.
ACS Chemical Biology 2017 December 16
Sublancin is a 37-amino acid antimicrobial peptide belonging to the glycocin family of natural products. It contains two helices that are held together by two disulfide bonds as well as an unusual S-glucosidic linkage to a Cys in a loop connecting the helices. We report the reconstitution of the biosynthetic pathway to this natural product in Escherichia coli. This technology enabled the evaluation of the structure-activity relationships of the solvent-exposed residues in the helices. The biosynthetic machinery proved tolerant of changes in both helices, and the bioactivity studies of the resulting mutants show that two residues in helix B are important for bioactivity, Asn31 and Arg33.
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