Experimental determination and computational interpretation of biophysical properties of lipid bilayers enriched by cholesteryl hemisuccinate
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
25450348
DOI
10.1016/j.bbamem.2014.10.032
PII: S0005-2736(14)00367-8
Knihovny.cz E-zdroje
- Klíčová slova
- Cholesterol-mimicking detergents, DPH, Dynamic light scattering, Laurdan, Molecular dynamics simulations, Time-dependent fluorescence shift,
- MeSH
- 2-naftylamin analogy a deriváty chemie MeSH
- cholesterol chemie MeSH
- dihydropyridiny chemie MeSH
- estery cholesterolu chemie MeSH
- fosfatidylcholiny chemie MeSH
- laurany chemie MeSH
- lipidové dvojvrstvy chemie MeSH
- liposomy chemie MeSH
- protony * MeSH
- simulace molekulární dynamiky MeSH
- voda chemie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- 1-palmitoyl-2-oleoylphosphatidylcholine MeSH Prohlížeč
- 1,2-oleoylphosphatidylcholine MeSH Prohlížeč
- 2-naftylamin MeSH
- 2,6-dimethyl-1,4-dihydropyridine-3,5-dicarboxylic acid monomethyl ester MeSH Prohlížeč
- cholesterol MeSH
- cholesteryl succinate MeSH Prohlížeč
- dihydropyridiny MeSH
- estery cholesterolu MeSH
- fosfatidylcholiny MeSH
- laurany MeSH
- laurdan MeSH Prohlížeč
- lipidové dvojvrstvy MeSH
- liposomy MeSH
- protony * MeSH
- voda MeSH
Cholesteryl hemisuccinate (CHS) is one of the cholesterol-mimicking detergents not observed in nature. It is, however, widely used in protein crystallography, in biochemical studies of proteins, and in pharmacology. Here, we performed an extensive experimental and theoretical study on the behavior of CHS in lipid membranes rich in unsaturated phospholipids. We found that the deprotonated form of CHS (that is the predominant form under physiological conditions) does not mimic cholesterol very well. The protonated form of CHS does better in this regard, but also its ability to mimic the physical effects of cholesterol on lipid membranes is limited. Overall, although ordering and condensing effects characteristic to cholesterol are present in systems containing any form of CHS, their strength is appreciably weaker compared to cholesterol. Based on the considerable amount of experimental and atomistic simulation data, we conclude that these differences originate from the fact that the ester group of CHS does not anchor it in an optimal position at the water-membrane interface. The implications of these findings for considerations of protein-cholesterol interactions are briefly discussed.
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