Pradimicin A, a D-mannose-binding antibiotic, binds pyranosides of L-fucose and L-galactose in a calcium-sensitive manner
Pradimicin A, a D-mannose-binding antibiotic, binds pyranosides of L-fucose and L-galactose in a calcium-sensitive manner
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Pradimicin A 是一种 D-甘露糖结合抗生素，以钙敏感方式结合 L-岩藻糖和 L-半乳糖的吡喃糖苷
DOI：
10.1016/j.bmcl.2015.05.021
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发表时间：
2015
期刊：
影响因子：
--
通讯作者：
M.
中科院分区：
文献类型：
--
作者：
Nakagawa;Y.;Watanabe;Y.;Igarashi;Y.;Ito;Y. and Ojika;M.
Pradimicin A (PRM-A) is a unique antibiotic with a lectin-like ability to bindd-mannose (d-Man) in the presence of Ca2+ion. Although accumulated evidences suggest that PRM-A recognizes the 2-, 3-, and 4-hydroxyl groups ofd-Man, BMY-28864, an artificial PRM-A derivative, was shown not to bindl-fucose (l-Fuc) andl-galactose (l-Gal), both of which share the characteristic array of the three hydroxyl groups withd-Man. To obtain a plausible explanation for this inconsistency, we performed co-precipitation experiments of PRM-A withl-Fuc,l-Gal, and their methyl pyranosides (l-Fuc-OMe,l-Gal-OMe) by taking advantage of aggregate-forming propensity of the binary [PRM-A/Ca2+] complex. Whilel-Fuc andl-Gal were hardly incorporated into the aggregate,l-Fuc-OMe andl-Gal-OMe were found to exhibit significant binding to PRM-A. However, increased Ca2+concentration abolished this binding, raising the possibility that poor binding ofl-Fuc andl-Gal to PRM-A is attributed to their chelation with Ca2+ion. This possibility was partly supported by1H NMR analysis that detected interaction ofl-Fuc andl-Gal with Ca2+ion in aqueous solution. These results collectively indicate that PRM-A binds pyranosides ofl-Fuc andl-Gal when Ca2+concentration is not excessive to trap these sugars by chelation but sufficient to form the [PRM-A/Ca2+] complex.
