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Titolo:
Interactions of the N-terminal domain of apolipoprotein E with a mimetic water-lipid surface: A molecular dynamics study
Autore:
Prevost, M; Ortmans, I;
Indirizzi:
Free Univ Brussels, B-1050 Brussels, Belgium Free Univ Brussels BrusselsBelgium B-1050 els, B-1050 Brussels, Belgium
Titolo Testata:
JOURNAL OF PHYSICAL CHEMISTRY B
fascicolo: 29, volume: 105, anno: 2001,
pagine: 7080 - 7086
SICI:
1520-6106(20010726)105:29<7080:IOTNDO>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR-BINDING DOMAIN; INDUCED CONFORMATIONAL-CHANGES; APOLIPOPHORIN-III; COMPUTER-SIMULATIONS; EXCHANGEABLE APOLIPOPROTEIN; CONTINUUM ELECTROSTATICS; HEXANE INTERFACE; MANDUCA-SEXTA; LIQUID WATER; ORIENTATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Prevost, M Free Univ Brussels, CP 165-64,Av F Roosevelt, B-1050 Brussels, Belgium Free Univ Brussels CP 165-64,Av F Roosevelt Brussels Belgium B-1050
Citazione:
M. Prevost e I. Ortmans, "Interactions of the N-terminal domain of apolipoprotein E with a mimetic water-lipid surface: A molecular dynamics study", J PHYS CH B, 105(29), 2001, pp. 7080-7086

Abstract

Apolipoprotein E, a protein that is subject to structural changes at a water/lipid interface, is studied by molecular dynamics simulations performed in water and at a water/organic-phase interface. The protein backbone atomsget significantly more hydrated in the interfacial system than in the water simulation and undergo larger positional fluctuations. Larger fluctuations and hydration concur to be more manifest in the interfacial region of theaqueous phase. In this interfacial region, water is more structured and makes, relative to its number of neighbors, more hydrogen bonds than water inthe bulk, a picture that has been previously inferred from molecular dynamics simulations of several water-organic liquid interfaces. We propose thatthe higher degree of protein hydration observed in the interfacial simulation arises from the structural behavior of interfacial water, which needs to make more H bonds and sees the protein as an additional partner. Our results are in agreement with spectroscopic data obtained for another apolipoprotein structurally similar to apolipoprotein E that show an increase in theprotein hydration in the presence of a water/lipid interface and suggest that hydration is a factor helping the barrier crossing from the structure in aqueous solution to a partially folded conformation prone to bind to the lipids.

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Documento generato il 20/01/20 alle ore 05:17:32