Immobilization of histidine-tagged proteins on monodisperse metallochelation liposomes: Preparation and study of their structure

0349452 - FZÚ 2011 RIV US eng J - Journal Article
Mašek, J. - Bartheldyová, E. - Korvasová, Z. - Škrabalová, J. - Koudelka, Š. - Kulich, P. - Kratochvílová, Irena - Miller, A. D. - Ledvina, Miroslav - Raška, M. - Turánek, J.
Immobilization of histidine-tagged proteins on monodisperse metallochelation liposomes: Preparation and study of their structure.
Analytical Biochemistry. Roč. 408, č. 1 (2011), s. 95-104. ISSN 0003-2697. E-ISSN 1096-0309
R&D Projects: GA ČR(CZ) GAP304/10/1951
Institutional research plan: CEZ:AV0Z10100520; CEZ:AV0Z40550506
Keywords : liposome * proteoliposome * detergent removal method * recombinant protein * metallochelatation * AF microscopy * TEM * dynamic light scattering
Subject RIV: CE - Biochemistry
Impact factor: 2.996, year: 2011

Liposomes represent a biocompatible platform for the construction of self-assembling proteoliposomes using nickel- or zinc-metallochelation. Here, we describe the design and construction of a flow-through ultrafiltration cell suitable for the preparation of monodisperse liposomes enabled for metallochelation and hence the formation of proteoliposomes. These model proteoliposomes are characterised by gel permeation chromatography and by dynamic light scattering. Transmission electron microscopy and immunogold staining are used to characterize surface bound proteins, revealing the tendency of rgp120 to form microdomains on liposome surfaces. These microdomains possess a 2D crystal-like structure that is seen more precisely by atomic force (AF) microscopy.
Permanent Link: http://hdl.handle.net/11104/0189688