Hydrophobic mismatch in gramicidin A'/Lecithin systems

Gramicidin A' (GA') has been added to three lipid systems of varying hydrophobic thicknesses: dimyristoyllecithin (DML), dipalmitoyllecithin (DPL), and distearoyllecithin (DSL). The similarity in length between the hydrophobic portion of GA' and the hydrocarbon chains of the lipid bil...

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Published in:Biochemistry
Main Authors: Watnick, Paula I., Chan, Sunney I., Dea, Phoebe
Format: Article in Journal/Newspaper
Language:unknown
Published: American Chemical Society 1990
Subjects:
DML
Online Access:https://doi.org/10.1021/bi00478a015
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spelling ftcaltechauth:oai:authors.library.caltech.edu:6fj1k-nt237 2024-10-06T13:48:14+00:00 Hydrophobic mismatch in gramicidin A'/Lecithin systems Watnick, Paula I. Chan, Sunney I. Dea, Phoebe 1990-07-03 https://doi.org/10.1021/bi00478a015 unknown American Chemical Society https://doi.org/10.1021/bi00478a015 eprintid:84796 info:eu-repo/semantics/closedAccess Other Biochemistry, 29(26), 6215-6221, (1990-07-03) info:eu-repo/semantics/article 1990 ftcaltechauth https://doi.org/10.1021/bi00478a015 2024-09-25T18:46:40Z Gramicidin A' (GA') has been added to three lipid systems of varying hydrophobic thicknesses: dimyristoyllecithin (DML), dipalmitoyllecithin (DPL), and distearoyllecithin (DSL). The similarity in length between the hydrophobic portion of GA' and the hydrocarbon chains of the lipid bilayers has been studied by using ^(31)P and ^2H NMR. Hydrophobic mismatch has been found to be most severe in the DML bilayer system and minimal in the case of DSL. In addition, the effects of hydrophobic mismatch on the cooperative properties of the bilayer have been obtained from ^2H NMR relaxation measurements. The results indicate that incorporation of the peptide into the bilayer disrupts the cooperative director fluctuations characteristic of pure multilamellar lipid dispersions. Finally, the GA'llecithin ratio at which the well-known transformation from bilayer to reverse hexagonal (H_(II)) phase occurs (Van Echteld et al., 1982; Chupin et al., 1987) is shown to depend on the acyl chain length of the phospholipid. A rationale is proposed for this chain length dependence. © 1990 American Chemical Society. Published in print 3 July 1990. Contribution No. 8343 of the Division of Chemistry and Chemical Engineering, California Institute of Technology. This work was supported by Grants GM-22432 (S.I.C.), GM-36132 (P.D.), and RR-08101 (P.D.) from the National Institutes of General Medical Sciences, US. Public Health Service, and by the donors of the Petroleum Research Fund, administered by the American Chemical Society. P.I.W. was a recipient of a National Research Service Award (T32 GM07616) from the National Institutes of General Medical Sciences. Access to the Southern California Regional NMR Facility at Caltech, supported by National Science Foundation Grant CHE84-40137, for the NMR experiments is gratefully acknowledged. We thank Drs. T. Handel, A. Nayeem, H. Eckert, and J. Yesinowski for helpful discussions and assistance. Article in Journal/Newspaper DML Caltech Authors (California Institute of Technology) Biochemistry 29 26 6215 6221
institution Open Polar
collection Caltech Authors (California Institute of Technology)
op_collection_id ftcaltechauth
language unknown
description Gramicidin A' (GA') has been added to three lipid systems of varying hydrophobic thicknesses: dimyristoyllecithin (DML), dipalmitoyllecithin (DPL), and distearoyllecithin (DSL). The similarity in length between the hydrophobic portion of GA' and the hydrocarbon chains of the lipid bilayers has been studied by using ^(31)P and ^2H NMR. Hydrophobic mismatch has been found to be most severe in the DML bilayer system and minimal in the case of DSL. In addition, the effects of hydrophobic mismatch on the cooperative properties of the bilayer have been obtained from ^2H NMR relaxation measurements. The results indicate that incorporation of the peptide into the bilayer disrupts the cooperative director fluctuations characteristic of pure multilamellar lipid dispersions. Finally, the GA'llecithin ratio at which the well-known transformation from bilayer to reverse hexagonal (H_(II)) phase occurs (Van Echteld et al., 1982; Chupin et al., 1987) is shown to depend on the acyl chain length of the phospholipid. A rationale is proposed for this chain length dependence. © 1990 American Chemical Society. Published in print 3 July 1990. Contribution No. 8343 of the Division of Chemistry and Chemical Engineering, California Institute of Technology. This work was supported by Grants GM-22432 (S.I.C.), GM-36132 (P.D.), and RR-08101 (P.D.) from the National Institutes of General Medical Sciences, US. Public Health Service, and by the donors of the Petroleum Research Fund, administered by the American Chemical Society. P.I.W. was a recipient of a National Research Service Award (T32 GM07616) from the National Institutes of General Medical Sciences. Access to the Southern California Regional NMR Facility at Caltech, supported by National Science Foundation Grant CHE84-40137, for the NMR experiments is gratefully acknowledged. We thank Drs. T. Handel, A. Nayeem, H. Eckert, and J. Yesinowski for helpful discussions and assistance.
format Article in Journal/Newspaper
author Watnick, Paula I.
Chan, Sunney I.
Dea, Phoebe
spellingShingle Watnick, Paula I.
Chan, Sunney I.
Dea, Phoebe
Hydrophobic mismatch in gramicidin A'/Lecithin systems
author_facet Watnick, Paula I.
Chan, Sunney I.
Dea, Phoebe
author_sort Watnick, Paula I.
title Hydrophobic mismatch in gramicidin A'/Lecithin systems
title_short Hydrophobic mismatch in gramicidin A'/Lecithin systems
title_full Hydrophobic mismatch in gramicidin A'/Lecithin systems
title_fullStr Hydrophobic mismatch in gramicidin A'/Lecithin systems
title_full_unstemmed Hydrophobic mismatch in gramicidin A'/Lecithin systems
title_sort hydrophobic mismatch in gramicidin a'/lecithin systems
publisher American Chemical Society
publishDate 1990
url https://doi.org/10.1021/bi00478a015
genre DML
genre_facet DML
op_source Biochemistry, 29(26), 6215-6221, (1990-07-03)
op_relation https://doi.org/10.1021/bi00478a015
eprintid:84796
op_rights info:eu-repo/semantics/closedAccess
Other
op_doi https://doi.org/10.1021/bi00478a015
container_title Biochemistry
container_volume 29
container_issue 26
container_start_page 6215
op_container_end_page 6221
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