@article{oai:nagoya.repo.nii.ac.jp:00028691,
 author = {Nakagawa, Yu and Doi, Takashi and Takegoshi, K. and Sugahara, Takahiro and Akase, Dai and Aida, Misako and Tsuzuki, Kazue and Watanabe, Yasunori and Tomura, Tomohiko and Ojika, Makoto and Igarashi, Yasuhiro and Hashizume, Daisuke and Ito, Yukishige},
 issue = {7},
 journal = {Cell Chemical Biology},
 month = {Jul},
 note = {Naturally occurring pradimicins (PRMs) show specific recognition of d-mannose (d-Man) in aqueous media, which has never been achieved by artificial small molecules. Although the Ca2+-mediated dimerization of PRMs is essential for their d-Man binding, the dimeric structure has yet to be elucidated, leaving the question open as to how PRMs recognize d-Man. Thus, we herein report the structural elucidation of the dimer by a combination of X-ray crystallography and solid-state NMR spectroscopy. Coupled with our previous knowledge regarding the d-Man binding geometry of PRMs, elucidation of the dimer allowed reliable estimation of the mode of d-Man binding. Based on the binding model, we further developed an azide-functionalized PRM derivative (PRM-Azide) with d-Man binding specificity. Notably, PRM-Azide stained Candida rugosa cells having mannans on their cell surface through conjugation with the tetramethylrhodamine fluorophore. The present study provides the practical demonstration that PRMs can serve as lectin mimics for use in glycobiological studies., ファイル公開：2020-07-18},
 pages = {950--959},
 title = {Molecular Basis of Mannose Recognition by Pradimicins and their Application to Microbial Cell Surface Imaging},
 volume = {26},
 year = {2019}
}