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Distinguishing bicontinuous lipid cubic phases from isotropic membrane morphologies using (31)P solid-state NMR spectroscopy.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yao, Hongwei Yang, Yu Hong, Mei
Description	Author Affiliation: Yang Y ( Department of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.); Yao H ( Department of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.); Hong M ( Department of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.)
Abstract	Nonlamellar lipid membranes are frequently induced by proteins that fuse, bend, and cut membranes. Understanding the mechanism of action of these proteins requires the elucidation of the membrane morphologies that they induce. While hexagonal phases and lamellar phases are readily identified by their characteristic solid-state NMR line shapes, bicontinuous lipid cubic phases are more difficult to discern, since the static NMR spectra of cubic-phase lipids consist of an isotropic (31)P or (2)H peak, indistinguishable from the spectra of isotropic membrane morphologies such as micelles and small vesicles. To date, small-angle X-ray scattering is the only method to identify bicontinuous lipid cubic phases. To explore unique NMR signatures of lipid cubic phases, we first describe the orientation distribution of lipid molecules in cubic phases and simulate the static (31)P chemical shift line shapes of oriented cubic-phase membranes in the limit of slow lateral diffusion. We then show that (31)P T2 relaxation times differ significantly between isotropic micelles and cubic-phase membranes: the latter exhibit 2 orders of magnitude shorter T2 relaxation times. These differences are explained by the different time scales of lipid lateral diffusion on the cubic-phase surface versus the time scales of micelle tumbling. Using this relaxation NMR approach, we investigated a DOPE membrane containing the transmembrane domain (TMD) of a viral fusion protein. The static (31)P spectrum of DOPE shows an isotropic peak, whose T2 relaxation times correspond to that of a cubic phase. Thus, the viral fusion protein TMD induces negative Gaussian curvature, which is an intrinsic characteristic of cubic phases, to the DOPE membrane. This curvature induction has important implications to the mechanism of virus-cell fusion. This study establishes a simple NMR diagnostic probe of lipid cubic phases, which is expected to be useful for studying many protein-induced membrane remodeling phenomena in biology.
ISSN	15206106
e-ISSN	15205207
Journal	The Journal of Physical Chemistry B
Issue Number	15
Volume Number	119
Language	English
Publisher	American Chemical Society (United States)
Publisher Date	2015-04-16
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Lipids Chemistry Membranes, Artificial Deuterium Magnetic Resonance Spectroscopy Micelles Parainfluenza Virus 5 Phase Transition Phosphatidylcholines Phosphatidylethanolamines Phosphatidylglycerols Phosphorus Radioisotopes Scattering, Small Angle Temperature Viral Fusion Proteins X-Ray Diffraction Research Support, N.I.H., Extramural Physical chemistry
Content Type	Text
Resource Type	Article
Subject	Surfaces, Coatings and Films Materials Chemistry Medicine Physical and Theoretical Chemistry

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