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Journal article

The impact of different phytosterols on the molecular dynamics in the hydrophobic/hydrophilic interface phosphatidylcholine- liposomes

From

Department of Systems Biology, Technical University of Denmark1

Plant sterols differ from cholesterol in having an alkyl group at Delta -24, and, in the case of stigmasterol, also a Delta -22 double bond. The effects of 10 mol% of three plant sterols (campesterol, fl-sitosterol, stigmasterol) and cholesterol on the molecular dynamics and phase behavior in multilamellar liposomes made from different phosphatidylcholine (PC) molecular species have been compared, utilizing the fluorescent probe Laurdan (2-dimethyl-amino-6-laurylnaphthalene).

Laurdan reports the molecular mobility in the hydrophilic/hydrophobic interface of the membrane by determining the rate of dipolar relaxation of water molecules close to the glycerol backbone of PC. Our results showed that the Delta -24 alkyl group of plant sterols did not affect their ability to reduce molecular mobility in this region of the PC membranes.

However, the plant sterols had a decreased capacity compared to cholesterol to inhibit formation of co-existing domains of gel and liquid-crystalline phases in membranes composed of equimolar dilauroyl-PC and dipalmitoyl-PC. The Delta -22 double bond present in stigmasterol decreased the ability of this sterol, compared to the other phytosterols, to reduce the molecular mobility at the hydrophobic/hydrophilic interface in membranes made of a saturated PC molecular species.

However, in membranes made from 16:0/18:2-PC, a lipid species common in plant plasma membranes, stigmasterol was as efficient as other sterols in affecting the polarity and molecular mobility at the hydrophilic /hydrophobic interface of the membrane at 25 degreesC, but was, in contrast to the other sterols, without effect at 0 degreesC.

Our results thus confirm as well as contradict the results of previous studies of the interactions between saturated PC and sterols, where other membrane regions were probed. The physiological relevance of the findings is discussed.

Language: English
Year: 2001
Pages: 23-32
ISSN: 13993054 and 00319317
Types: Journal article
DOI: 10.1034/j.1399-3054.2001.1130104.x
Keywords

protein

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