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Molecular insight into the electrostatic membrane surface potential by 14n/31p MAS NMR spectroscopy: nociceptin-lipid association

Molecular insight into the electrostatic membrane surface potential by 14n/31p MAS NMR spectroscopy: nociceptin-lipid association
Molecular insight into the electrostatic membrane surface potential by 14n/31p MAS NMR spectroscopy: nociceptin-lipid association
Exploiting naturally abundant 14N and 31P nuclei by high-resolution MAS NMR (magic angle spinning nuclear magnetic resonance) provides a molecular view of the electrostatic potential present at the surface of biological model membranes, the electrostatic charge distribution across the membrane interface, and changes that occur upon peptide association. The spectral resolution in 31P and 14N MAS NMR spectra is sufficient to probe directly the negatively charged phosphate and positively charged choline segment of the electrostatic P--O-CH2-CH2-N+(CH3)3 headgroup dipole of zwitterionic DMPC (dimyristoylphosphatidylcholine) in mixed-lipid systems. The isotropic shifts report on the size of the potential existing at the phosphate and ammonium group within the lipid headgroup while the chemical shielding anisotropy (31P) and anisotropic quadrupolar interaction (14N) characterize changes in headgroup orientation in response to surface potential. The 31P/14N isotropic chemical shifts for DMPC show opposing systematic changes in response to changing membrane potential, reflecting the size of the electrostatic potential at opposing ends of the P--N+ dipole. The orientational response of the DMPC lipid headgroup to electrostatic surface variations is visible in the anisotropic features of 14N and 31P NMR spectra. These features are analyzed in terms of a modified "molecular voltmeter" model, with changes in dynamic averaging reflecting the tilt of the C-N+(CH)3 choline and PO4- segment. These properties have been exploited to characterize the changes in surface potential upon the binding of nociceptin to negatively charged membranes, a process assumed to proceed its agonistic binding to its opoid G-protein coupled receptor.
0002-7863
6610-6616
Lindström, Fredrick
994533ee-f05c-48b7-88b4-a686677b5ec9
Williamson, Philip T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Gröbner, Gerhard
daa0d5a7-fb05-483c-94e7-23e9c6a3c835
Lindström, Fredrick
994533ee-f05c-48b7-88b4-a686677b5ec9
Williamson, Philip T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Gröbner, Gerhard
daa0d5a7-fb05-483c-94e7-23e9c6a3c835

Lindström, Fredrick, Williamson, Philip T.F. and Gröbner, Gerhard (2005) Molecular insight into the electrostatic membrane surface potential by 14n/31p MAS NMR spectroscopy: nociceptin-lipid association. Journal of the American Chemical Society, 127 (18), 6610-6616. (doi:10.1021/ja042325b).

Record type: Article

Abstract

Exploiting naturally abundant 14N and 31P nuclei by high-resolution MAS NMR (magic angle spinning nuclear magnetic resonance) provides a molecular view of the electrostatic potential present at the surface of biological model membranes, the electrostatic charge distribution across the membrane interface, and changes that occur upon peptide association. The spectral resolution in 31P and 14N MAS NMR spectra is sufficient to probe directly the negatively charged phosphate and positively charged choline segment of the electrostatic P--O-CH2-CH2-N+(CH3)3 headgroup dipole of zwitterionic DMPC (dimyristoylphosphatidylcholine) in mixed-lipid systems. The isotropic shifts report on the size of the potential existing at the phosphate and ammonium group within the lipid headgroup while the chemical shielding anisotropy (31P) and anisotropic quadrupolar interaction (14N) characterize changes in headgroup orientation in response to surface potential. The 31P/14N isotropic chemical shifts for DMPC show opposing systematic changes in response to changing membrane potential, reflecting the size of the electrostatic potential at opposing ends of the P--N+ dipole. The orientational response of the DMPC lipid headgroup to electrostatic surface variations is visible in the anisotropic features of 14N and 31P NMR spectra. These features are analyzed in terms of a modified "molecular voltmeter" model, with changes in dynamic averaging reflecting the tilt of the C-N+(CH)3 choline and PO4- segment. These properties have been exploited to characterize the changes in surface potential upon the binding of nociceptin to negatively charged membranes, a process assumed to proceed its agonistic binding to its opoid G-protein coupled receptor.

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Published date: 13 April 2005
Organisations: Biological Sciences

Identifiers

Local EPrints ID: 45399
URI: https://eprints.soton.ac.uk/id/eprint/45399
ISSN: 0002-7863
PURE UUID: 2d01e81d-b9e1-46e0-855b-c3145a8f2da5
ORCID for Philip T.F. Williamson: ORCID iD orcid.org/0000-0002-0231-8640

Catalogue record

Date deposited: 27 Mar 2007
Last modified: 20 Jul 2019 00:53

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Author: Fredrick Lindström
Author: Gerhard Gröbner

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