Fluorinated cholesterol retains domain-forming activity in sphingomyelin bilayers

Nobuaki Matsumori, Horoki Okazaki, Kaoru Nomura, Michio Murata

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Lipid rafts are cholesterol (Chol)-rich microdomains floating in a sea of lipid bilayers. Chol is thought to interact preferentially with sphingolipids such as sphingomyelin (SM) rather than with glycerophospholipids, and this putative SM-Chol interaction is generally recognized as a requirement for raft formation. However, the presence of the specific interaction is still controversial, primarily because of the lack of useful molecular probes for scrutinizing this interaction. Recently, we reported that the dynamic properties of 6-F-Chol in DMPC bilayers are similar to those of unmodified Chol. Hence, in the present study, we first compared the roles of 6-F-Chol and Chol in SM bilayers through detergent insolubility, fluorescence polarization, and 2H NMR experiments. The results demonstrated that 6-F-Chol and Chol behave similarly in SM bilayers, whereas, in SM-DOPC membranes, 6-F-Chol is less effective in domain formation. Then, we analyzed the molecular orientation of 6-F-Chol in SM bilayers using solid-state NMR, and found that the dynamics and orientation of 6-F-Chol in SM bilayers are almost identical to those in DMPC bilayers. This supports the notion of the lack of a putative specific interaction between SM and Chol. Thus, this study demonstrates the utility of 6-F-Chol as a molecular probe for understanding molecular recognition in lipid rafts.

Original languageEnglish
Pages (from-to)401-408
Number of pages8
JournalChemistry and Physics of Lipids
Volume164
Issue number5
DOIs
Publication statusPublished - Jul 2011

Fingerprint

Sphingomyelins
Cholesterol
Dimyristoylphosphatidylcholine
Molecular Probes
Nuclear magnetic resonance
Glycerophospholipids
Lipids
Molecular recognition
Sphingolipids
Lipid bilayers
Fluorescence Polarization
Molecular orientation
Lipid Bilayers
Detergents

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Cell Biology

Cite this

Fluorinated cholesterol retains domain-forming activity in sphingomyelin bilayers. / Matsumori, Nobuaki; Okazaki, Horoki; Nomura, Kaoru; Murata, Michio.

In: Chemistry and Physics of Lipids, Vol. 164, No. 5, 07.2011, p. 401-408.

Research output: Contribution to journalArticle

Matsumori, Nobuaki ; Okazaki, Horoki ; Nomura, Kaoru ; Murata, Michio. / Fluorinated cholesterol retains domain-forming activity in sphingomyelin bilayers. In: Chemistry and Physics of Lipids. 2011 ; Vol. 164, No. 5. pp. 401-408.
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