Utilizing adsorbed proteoliposomes trapped in a non-ruptured state on SiO2 for amplified detection of membrane proteins
Artikel i vetenskaplig tidskrift, 2004

The quartz crystal microbalance with dissipation (QCM-D) technique was used to monitor the formation of supported phospholipid bilayers (SPBs) on SiO2 using proteoliposomes with reconstituted proton translocating nicotinamide nucleotide transhydrogenase (TH). Exposure of the surface to such proteoliposomes creates a lipid film composed of a mixture of proteolipid bilayers and adsorbed non-ruptured proteoliposomes, where the fraction of the latter is reduced if the TH-liposomes are pretreated with trypsin to remove the water soluble domains of TH [Langmuir 19 (2003) 842]. In the present work, the latter study is complemented by investigating the influence of trypsin treatment of the mixed adlayer (proteolipid bilayer + non-ruptured proteoliposomes) after adsorption on the surface. This demonstrates how trypsin-cleavage induced rupture of adsorbed TH-liposomes can be utilized to detect the presence of less than 0.04 pmol/cm2 of immobilized TH.

QCM-D

SPR

Lipids

Transmembrane proteins

Supported membranes

Författare

Annette Granéli

Chalmers, Teknisk fysik

Jan Rydström

Göteborgs universitet

Bengt Herbert Kasemo

Chalmers, Teknisk fysik, Kemisk fysik

Fredrik Höök

Chalmers, Teknisk fysik, Kemisk fysik

Biosensors and Bioelectronics

0956-5663 (ISSN)

Vol. 20 3 498-504

Ämneskategorier

Biokemi och molekylärbiologi

Fysik

DOI

10.1016/j.bios.2004.02.013

PubMed

15494231