Surface thermodynamic properties of monolayers versus reconstitution of a membrane protein in solid-supported bilayers

Surface thermodynamic properties of monolayers versus reconstitution of a membrane protein in solid-supported bilayers
Engineering Village 2
? 2006 Elsevier Inc
Accession number: 05339305847

Title: Surface thermodynamic properties of monolayers versus reconstitution of a membrane protein in solid-supported bilayers

Authors: Merino, Sandra; Domenech, Oscar; Diez-Perez, Ismael; Sanz, Fausto; Montero, M. Teresa; Hernandez-Borrell, Jordi

Author affiliation: Departament de Fisicoquimica, Facultat de Farmacia, Universitat de Barcelona, 08028 Barcelona, Spain

Serial title: Colloids and Surfaces B: Biointerfaces

Abbreviated serial title: Colloids Surf. B Biointerfaces

Volume: v 44

Issue: n 2-3

Issue date: August 2005

Publication year: 2005

Pages: p 93-98

Language: English

ISSN: 0927-7765

CODEN: CSBBEQ

Document type: Journal article (JA)

Publisher: Elsevier, Amsterdam, 1000 AE, Netherlands

Abstract: Atomic force microscopy (AFM) was used to study the influence of a membrane protein, lactose permease of Escherichia coli (LacY), on the surface spreading behavior and the features of self-assembled phospholipids bilayers on mica. The miscibility of phospholipids used, 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), was investigated by surface pressure area isotherm measurements at the air-water interface. A composition with an equimolar proportion of POPC and DMPC was used to form the liposomes. Surface layers formed with DMPC:POPC (0.5:0.5, mol/mol) or LacY reconstituted in proteoliposomes with the same phospholipid composition were imaged by using AFM. When lactose permease was reconstituted in DMPC:POPC (0.5:0.5, mol/mol), self-assembled structures that remained firmly adsorbed onto the mica surface were observed. These sheets had an irregular shape and their upper layer was more corrugated than that obtained for the phospholipid matrix. ? 2005 Elsevier B.V. All rights reserved.

Number of references: 31

Ei main heading: Thermodynamic properties

Ei controlled terms: Monolayers - Proteins - Escherichia coli - Enzymes - Phospholipids - Mica - Isotherms - Solubility - Atomic force microscopy

Uncontrolled terms: Lactose permease - Bilayers - Proteoliposomes - Phospholipid matrix

Ei classification codes: 641.1 Thermodynamics - 813.2 Coating Materials - 804.1 Organic Compounds - 461.9 Biology - 461.2 Biological Materials - 482.2 Minerals - 801.4 Physical Chemistry - 741.3 Optical Devices & Systems - 931.3 Atomic & Molecular Physics

Treatment: Experimental (EXP)

DOI: 10.1016/j.colsurfb.2005.06.003

Database: Compendex

Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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