期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 140, 期 11, 页码 3892-3906出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b06863
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资金
- Institute for Collaborative Biotechnologies through U.S. Army Research Office [W911NF-09-0001]
- National Institutes of Health [R01GM116128]
- MRSEC program of the US NSF [DMR-1720256]
- CONVENE-IGERT program of the U.S. National Science Foundation [NSF-DGE 0801627]
- Alexander von Humboldt-Foundation through a Feodor Lynen Research Fellowship
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM116128] Funding Source: NIH RePORTER
A versatile synthetic protocol is reported that allows high concentrations of functionally active membrane proteins to be incorporated in mesostructured silica materials. Judicious selections of solvent, surfactant, silica precursor species, and synthesis conditions enable membrane proteins to be stabilized in solution and during subsequent coassembly into silica-surfactant composites with nano- and mesoscale order. This was demonstrated by using a combination of nonionic (n-dodecyl-beta-D-maltoside or Pluronic P123), lipid-like (1,2-diheptanoyl-sn-glycero-3-phosphocholine), and perfluoro-octanoate surfactants under mild acidic conditions to coassemble the light-responsive transmembrane protein proteorhodopsin at concentrations up to 15 wt % into the hydrophobic regions of worm-like mesostructured silica materials in films. Small-angle X-ray scattering, electron paramagnetic resonance spectroscopy, and transient UV-visible spectroscopy analyses established that proteorhodopsin molecules in mesostructured silica films exhibited native-like function, as well as enhanced thermal stability compared to surfactant or lipid environments. The light absorbance properties and light-activated conformational changes of proteorhodopsin guests in mesostructured silica films are consistent with those associated with the native H+-pumping mechanism of these biomolecules. The synthetic protocol is expected to be general, as demonstrated also for the incorporation of functionally active cytochrome c, a peripheral membrane protein enzyme involved in electron transport, into mesostructured silica-cationic surfactant films.
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