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Precursor-directed biosynthesis and biological activity of tripropeptin Cpip, a new tripropeptin C analog containing pipecolic acid.
J Antibiot (Tokyo)
April 2024
Laboratory of Microbiology, Institute of Microbial Chemistry (BIKAKEN), Tokyo, 3-14-23 Kamiosaki, Shinagawa-ku, Tokyo, 141-0021, Japan.
Article Synopsis
- Tripropeptin C is a cyclic lipopeptide that effectively fights against methicillin-resistant Staphylococcus aureus in mice.
- Researchers replaced proline residues in tripropeptin C with pipecolic acid to explore its impact on antibacterial activity.
- The modified analog, tripropeptin Cpip, displayed significantly weaker efficacy against Gram-positive bacteria, indicating that the original proline structure is crucial for the compound's antibacterial potency.
Genome Sequence of sp. Strain BMK333-48F3, the Producer Strain of Potent Lipopeptide Antibiotics of the Tripropeptin Family.
Microbiol Resour Announc
December 2021
Department of Pharmaceutical Biology, Pharmaceutical Institute, University of Tübingen, Tübingen, Germany.
sp. strain BMK333-48F3 is known primarily for its production of the antibiotically active tripropeptins. Here, we report its draft genome sequence, which will give insight into the biosynthesis of tripropeptins and enable genome mining for further secondary metabolites.
View Article and Find Full Text PDFIn vivo efficacy of β-lactam/tripropeptin C in a mouse septicemia model and the mechanism of reverse β-lactam resistance in methicillin-resistant Staphylococcus aureus mediated by tripropeptin C.
J Antibiot (Tokyo)
July 2017
Laboratory of Microbiology, Institute of Microbial Chemistry (BIKAKEN), Tokyo, Japan.
Natural lipopeptide antibiotic tripropeptin C (TPPC) revitalizes and synergistically potentiates the activities of the class of β-lactam antibiotics against methicillin-resistant Staphylococcus aureus (MRSA) but not against methicillin-sensitive S. aureus in vitro; however, the mode of action remains unclear. In the course of the study to reveal its mode of action, we found that TPPC inhibited the β-lactamase production induced by cefotiam.
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