TY - JOUR
T1 - Membrane interaction of amphotericin B as single-length assembly examined by solid state NMR for uniformly 13C-enriched agent
AU - Matsuoka, Shigeru
AU - Ikeuchi, Hiroki
AU - Umegawa, Yuichi
AU - Matsumori, Nobuaki
AU - Murata, Michio
N1 - Funding Information:
The present work was supported by Grants-in-Aid for Scientific Research (A) (No. 15201048), and for Scientific Research on Priority Area (A) (No. 16073211) from MEXT, Japan; by a grant from the CREST, Japan Science and Technology Corporation, and by the Yamada Science Foundation. We are grateful to Prof. Yuzuru Mikami, Research Center for Pathogenic Fungi and Microbial Toxicoses, Chiba University, for antifungal assays; to Prof. Tohru Oishi for discussion; and to Mutsuhiro Ohata and Satoru Ujihara for their help in cultures of microorganism.
PY - 2006/10/1
Y1 - 2006/10/1
N2 - The membrane interaction of amphotericin B (AmB), one of the most important anti-fungal drugs, was investigated by solid state NMR measurements of uniformly 13C-enriched AmB, which was prepared by the culture of the drug-producing microorganism in the presence of [u-13C6]glucose. All the 13C NMR signals of AmB upon binding to DLPC membrane were successfully assigned on the basis of the 13C-13C correlation spectrum. 13C-31P RDX (Rotational-Echo Double Resonance for X-clusters) experiments clearly revealed the REDOR dephasing effects for carbon atoms residing in the both terminal parts, whereas no dephasing was observed for the middle parts including polyolefinic C20-C33 and hydroxyl-bearing C8/C9 parts. These observations suggest that AmB binds to DLPC membrane with a high affinity to the phospholipid and spans the membrane with a single molecular length.
AB - The membrane interaction of amphotericin B (AmB), one of the most important anti-fungal drugs, was investigated by solid state NMR measurements of uniformly 13C-enriched AmB, which was prepared by the culture of the drug-producing microorganism in the presence of [u-13C6]glucose. All the 13C NMR signals of AmB upon binding to DLPC membrane were successfully assigned on the basis of the 13C-13C correlation spectrum. 13C-31P RDX (Rotational-Echo Double Resonance for X-clusters) experiments clearly revealed the REDOR dephasing effects for carbon atoms residing in the both terminal parts, whereas no dephasing was observed for the middle parts including polyolefinic C20-C33 and hydroxyl-bearing C8/C9 parts. These observations suggest that AmB binds to DLPC membrane with a high affinity to the phospholipid and spans the membrane with a single molecular length.
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U2 - 10.1016/j.bmc.2006.06.001
DO - 10.1016/j.bmc.2006.06.001
M3 - Article
C2 - 16782343
AN - SCOPUS:33747157259
VL - 14
SP - 6608
EP - 6614
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
SN - 0968-0896
IS - 19
ER -