Ergosterol increases the intermolecular distance of amphotericin B in the membrane-bound assembly as evidenced by solid-state NMR

Yuichi Umegawa, Nobuaki Matsumori, Tohru Oishi, Michio Murata

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Amphotericin B (AmB) exerts its antifungal activity by forming ion-permeable assemblies across lipid bilayers. To investigate AmB-AmB bimolecular interactions in the assembly, we carried out 13C{ 19F}REDOR experiments using 14-19F- and 13C41-labeled AmBs in sterol-containing and sterol-free palmitoyloleoylphosphatidylcholine (POPC) membranes and measured the average distance between the labeled sites of AmBs in membrane-bound forms. The REDOR results suggested that the intermolecular distance of AmB molecules is significantly increased in the ergosterol membrane as compared with the cholesterol membrane. This sterol-dependent change was supported by the UV spectra of AmB in lipid bilayers, in which the excitonic absorption band arising from the aggregated state of AmB shifted to longer wavelength in ergosterol-containing POPC membrane. The REDOR experiments also disclosed that the head-to-head orientation of AmB is predominant in both of the sterol-containing membranes and AmB-POPC interaction was detected only in the ergosterol membrane. Ergosterol significantly influences the interactions between AmB molecules as well as those between AmB and POPC, which may facilitate formation of ion-permeable channels in ergosterol-containing membrane.

Original languageEnglish
Pages (from-to)13463-13469
Number of pages7
JournalBiochemistry
Volume47
Issue number51
DOIs
Publication statusPublished - Dec 23 2008
Externally publishedYes

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Ergosterol
Amphotericin B
Nuclear magnetic resonance
Membranes
Sterols
Lipid bilayers
Lipid Bilayers
Ions
Molecules
Ion Channels
Absorption spectra
Experiments
Cholesterol

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Ergosterol increases the intermolecular distance of amphotericin B in the membrane-bound assembly as evidenced by solid-state NMR. / Umegawa, Yuichi; Matsumori, Nobuaki; Oishi, Tohru; Murata, Michio.

In: Biochemistry, Vol. 47, No. 51, 23.12.2008, p. 13463-13469.

Research output: Contribution to journalArticle

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