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Solid state N-14 and P-31 MAS NMR: new tools to study electrostatic binding of peptides on biomembrane surfaces.

Solid state N-14 and P-31 MAS NMR: new tools to study electrostatic binding of peptides on biomembrane surfaces.
Solid state N-14 and P-31 MAS NMR: new tools to study electrostatic binding of peptides on biomembrane surfaces.
The effect of electrostatic peptide association via its basic residues on lipid headgroup orientation in biological lipid membranes was investigated by monitoring both 14N and 31P nuclear magnetic resonance (NMR) spectroscopy. Lipid membranes were in the liquid crystalline phase at 308K and consisted of anionic DMPG or cationic DDAB added to neutral DMPC at different ratios to but also by ternary lipid bilayers with zero nominal surface charge. The quadrupolar splitting of the 14N nucleus and the isotropic chemical shift value of the 31P nucleus shows a systematic response to changes in the surface electrostatic charge. Also by utilizing the naturally occurring spin reporters 14N and 31P both parts of the choline headgroup electric dipole P---N+(CH3)3 can be observed. This approach provides information about association between lipid bilayers and proteins but also changes in the headgroup surrounding electrostatic environment. Previous results indicate that the interaction between pentalysine, a highly basic peptide with five positive charges, and lipid membranes is purely electrostatic. By adding pentalysine to membranes at different ratios the response of the lipid headgroup to pure electrostatic peptide association could be determined.
0006-3495
19A-19A
Lindstrom, Fredrik
b8ff852c-551f-4dfd-8aeb-792475654b80
Sani, Marco.
b1f9ef9b-f182-4ca5-bad8-cf9e16d968cc
Williamson, Philip.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Bokvist, Marcus
73e41153-6320-4c4a-be51-5b7559de3c99
Grobner, Gerhad
22f0b42e-e6bf-4908-a421-c1fda0de2cf0
Lindstrom, Fredrik
b8ff852c-551f-4dfd-8aeb-792475654b80
Sani, Marco.
b1f9ef9b-f182-4ca5-bad8-cf9e16d968cc
Williamson, Philip.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Bokvist, Marcus
73e41153-6320-4c4a-be51-5b7559de3c99
Grobner, Gerhad
22f0b42e-e6bf-4908-a421-c1fda0de2cf0

Lindstrom, Fredrik, Sani, Marco., Williamson, Philip.T.F., Bokvist, Marcus and Grobner, Gerhad (2004) Solid state N-14 and P-31 MAS NMR: new tools to study electrostatic binding of peptides on biomembrane surfaces. Biophysical Journal, 86 (1), 19A-19A.

Record type: Article

Abstract

The effect of electrostatic peptide association via its basic residues on lipid headgroup orientation in biological lipid membranes was investigated by monitoring both 14N and 31P nuclear magnetic resonance (NMR) spectroscopy. Lipid membranes were in the liquid crystalline phase at 308K and consisted of anionic DMPG or cationic DDAB added to neutral DMPC at different ratios to but also by ternary lipid bilayers with zero nominal surface charge. The quadrupolar splitting of the 14N nucleus and the isotropic chemical shift value of the 31P nucleus shows a systematic response to changes in the surface electrostatic charge. Also by utilizing the naturally occurring spin reporters 14N and 31P both parts of the choline headgroup electric dipole P---N+(CH3)3 can be observed. This approach provides information about association between lipid bilayers and proteins but also changes in the headgroup surrounding electrostatic environment. Previous results indicate that the interaction between pentalysine, a highly basic peptide with five positive charges, and lipid membranes is purely electrostatic. By adding pentalysine to membranes at different ratios the response of the lipid headgroup to pure electrostatic peptide association could be determined.

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More information

Published date: 1 January 2004

Identifiers

Local EPrints ID: 56565
URI: http://eprints.soton.ac.uk/id/eprint/56565
ISSN: 0006-3495
PURE UUID: 454f8cd5-04b3-4f01-ad83-4bca4f9b46c7
ORCID for Philip.T.F. Williamson: ORCID iD orcid.org/0000-0002-0231-8640

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Date deposited: 11 Aug 2008
Last modified: 12 Dec 2021 03:36

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Contributors

Author: Fredrik Lindstrom
Author: Marco. Sani
Author: Marcus Bokvist
Author: Gerhad Grobner

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