Physicochemical Studies of Bacteriorhodopsin Reconstituted in Partially Fluorinated Phosphatidylcholine Bilayers
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- Masaru Yoshino
- Department of Chemistry and Chemical Biology, Graduate School of Engineering, Gunma University, Kiryu 376-8515, Japan
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- Takashi Kikukawa
- Faculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan
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- Hiroshi Takahashi
- Department of Chemistry and Chemical Biology, Graduate School of Engineering, Gunma University, Maebashi 371-8510, Japan
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- Toshiyuki Takagi
- Research Center for Stem Cell Engineering, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba 305-8565, Japan
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- Yasunori Yokoyama
- Department of Applied Physics, Graduate School of Engineering, Nagoya University, Nagoya 464-8603, Japan
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- Hideki Amii
- Department of Chemistry and Chemical Biology, Graduate School of Engineering, Gunma University, Kiryu 376-8515, Japan
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- Teruhiko Baba
- Research Center for Stem Cell Engineering, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba 305-8565, Japan
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- Toshiyuki Kanamori
- Research Center for Stem Cell Engineering, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba 305-8565, Japan
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- Masashi Sonoyama
- Department of Chemistry and Chemical Biology, Graduate School of Engineering, Gunma University, Kiryu 376-8515, Japan
書誌事項
- 公開日
- 2013-04-29
- 資源種別
- journal article
- DOI
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- 10.1021/jp311665z
- 公開者
- American Chemical Society (ACS)
この論文をさがす
説明
A membrane protein bacteriorhodopsin (bR) that is successfully reconstituted in liposome of a novel partially fluorinated analog of dimyristoylphosphatidylcholine (DMPC) with the perfluorobutyl segments in the myristoyl groups, diF4H10-PC, has been investigated by some spectroscopic and X-ray diffraction techniques to clarify effects of substitution of nine hydrogen atoms by fluorine atoms on structural and physical properties of the membrane protein by comparison with the previous results on proteoliposome of bR and DMPC. Below the gel-to-liquid crystalline phase transition of diF4H10-PC bilayer, bR molecules adopt the two-dimensional lattice structure of trimers as the structural unit and show a photocycle very similar to that of native purple membrane like reconstituted bR in DMPC liposome in the gel phase. Even upon heating up to temperatures well above the phase transition, the nativelike functional reconstitution and higher structural stability of bR molecules in diF4H10-PC liposome are retained, which strikingly contrasts with lipid phase transition-induced disaggregation of protein molecules and light-induced denaturation in DMPC liposome. Greater membrane rigidity and low affinity between bR and fluorinated lipid molecules are proposed as a driving force for keeping nativelike properties of bR molecules in diF4H10-PC liposome even in the fluid phase.
収録刊行物
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- The Journal of Physical Chemistry B
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The Journal of Physical Chemistry B 117 (18), 5422-5429, 2013-04-29
American Chemical Society (ACS)
