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Updated: Jun 11, 2026

Nanomechanics of Drug-target Interactions and Antibacterial Resistance Detection
Published on: October 25, 2013
Inactivation of P450 Reprograms the Ring Topology of Glycopeptide Antibiotics
Mingzhu Mao1,2, Xingkun Li2,3, Weiqian Qi1,2
1College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China.
Abstract:
Glycopeptide antibiotics (GPAs) are the drugs of choice for life-threatening Gram-positive infections and feature a biphenolic coupling cross-linked peptide scaffold constructed by certain P450s in a strict sequence- and position-specific manner. However, in situ point mutation of P450 within the fumamycin biosynthetic gene cluster uncovered new derivatives possessing previously inaccessible cross-link patterns, suggesting that P450 inactivation can reprogram the ring topology of GPAs and thereby could be used to expand their chemical space.
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