TY - JOUR
T1 - Channels formed by amphotericin B covalent dimers exhibit rectification
AU - Hirano, Minako
AU - Takeuchi, Yuko
AU - Matsumori, Nobuaki
AU - Murata, Michio
AU - Ide, Toru
N1 - Funding Information:
We thank Prof. P. Karagiannis for carefully revising the manuscript. This work was supported by grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan (Innovative Nanoscience of Supermolecular Motor Proteins Working in Biomembranes, Molecular Science of Fluctuations toward Biological Functions and Molecular System Life Science).
PY - 2011/4
Y1 - 2011/4
N2 - Amphotericin B (AmB) is a widely used antifungal antibiotic with high specificity for fungi. We previously synthesized several covalently conjugated AmB dimers to clarify the AmB channel structure. Among these dimers, that with an aminoalkyl linker was found to exhibit potent hemolytic activity. We continue this work by investigating the channel activity of the dimer, finding that all channels comprised of AmB dimers show rectification. The direction of the dimer channel in the membrane depended on the electric potential at which the dimer channel was formed. On the other hand, only about half the monomer channels showed rectification. In addition, these channels were easily switched from a rectified to a nonrectified state following voltage stimulation, indicating instability. We propose a model to describe the AmB channel structure that explains why AmB dimer channels necessarily show rectification.
AB - Amphotericin B (AmB) is a widely used antifungal antibiotic with high specificity for fungi. We previously synthesized several covalently conjugated AmB dimers to clarify the AmB channel structure. Among these dimers, that with an aminoalkyl linker was found to exhibit potent hemolytic activity. We continue this work by investigating the channel activity of the dimer, finding that all channels comprised of AmB dimers show rectification. The direction of the dimer channel in the membrane depended on the electric potential at which the dimer channel was formed. On the other hand, only about half the monomer channels showed rectification. In addition, these channels were easily switched from a rectified to a nonrectified state following voltage stimulation, indicating instability. We propose a model to describe the AmB channel structure that explains why AmB dimer channels necessarily show rectification.
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U2 - 10.1007/s00232-011-9354-x
DO - 10.1007/s00232-011-9354-x
M3 - Article
C2 - 21424544
AN - SCOPUS:79953728167
SN - 0022-2631
VL - 240
SP - 159
EP - 164
JO - Journal of Membrane Biology
JF - Journal of Membrane Biology
IS - 3
ER -