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- W1990802611 abstract "Pradimicin A (PRM-A) is a unique antibiotic with a lectin-like ability to recognize d-mannopyranosides (Man) in the presence of Ca2+ ion. BMY-28864 (1) is a water-soluble analogue of PRM-A, which has been extensively used for studies on the mode of Man recognition and antifungal action of pradimicins. Although it has been assumed that PRM-A and 1 bind Man in a similar fashion, direct experimental evidence has yet to be provided. In this report, we compared Ca2+ and Man binding of 1 with that of PRM-A through two solid-state NMR experiments. The solid-state 113Cd NMR analysis using 113Cd2+ ion as a surrogate for Ca2+ ion suggested the similarity in Ca2+ coordination of PRM-A and 1. The dipolar assisted rotational resonance (DARR) analysis using 13C-labeled 1 clearly showed that 1 as well as PRM-A binds Man near its carboxyl group. These results collectively indicate that the mode of binding of Ca2+ ion and Man is nearly identical between PRM-A and 1." @default.
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- W1990802611 date "2012-01-01" @default.
- W1990802611 modified "2023-10-18" @default.
- W1990802611 title "Solid-state NMR analysis of calcium and d-mannose binding of BMY-28864, a water-soluble analogue of pradimicin A" @default.
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- W1990802611 doi "https://doi.org/10.1016/j.bmcl.2011.11.106" @default.
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