1359668-28-2Relevant academic research and scientific papers
Solid-state NMR analysis of calcium and D-mannose binding of BMY-28864, a water-soluble analogue of pradimicin A
Nakagawa, Yu,Doi, Takashi,Takegoshi,Igarashi, Yasuhiro,Ito, Yukishige
, p. 1040 - 1043 (2012)
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 Ca 2+ ion and Man is nearly identical between PRM-A and 1.
