Phospholipid/cholesterol/decanethiol mixtures for direct assembly of immunosensing interfaces

被引:7
作者
Almeida, I. [1 ]
Marques, J. T. [1 ]
Liu, W. [2 ]
Niu, Y. [2 ]
de Almeida, R. F. M. [1 ]
Jin, G. [2 ]
Viana, A. S. [1 ]
机构
[1] Univ Lisbon, Fac Ciencias, Ctr Quim & Bioquim, Edificio C8, P-1749016 Lisbon, Portugal
[2] Chinese Acad Sci, Inst Mech, Beijing 100190, Peoples R China
关键词
Planar hybrid supported lipid bilayers; Thiol-gold linkages; Antibody covalent coupling; Inhibition of nonspecific adsorption; Immunosensors; Surface plasmon resonance; BILAYER-LIPID MEMBRANES; PHASE-EQUILIBRIA; MODIFIED GOLD; CHOLESTEROL; IMMOBILIZATION; PHOSPHATIDYLCHOLINE; ADSORPTION; DISULFIDE; RESONANCE; VESICLES;
D O I
10.1016/j.colsurfb.2015.10.048
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
In this work, a simple yet robust method to prepare lipid-based biosensing interfaces on gold using common lipids (a phospholipid and cholesterol) and an alkanethiol is reported. The lipids were carefully chosen to tailor the biophysical properties of the bilayer. The simplicity of the method relies on the incorporation of a small percentage of decanethiol in the lipid vesicles for a direct formation of a thiol-linked supported lipid bilayer, which is advantageous in several respects. It prevents the use of specially synthesized thiolipids and preserves the natural fluidity and dynamics of the lipids. As a consequence the whole arrangement is extremely stable regarding ionic strength changes and solution flow during surface plasmon resonance experiments. Moreover, we show that this interface is very effective on suppressing the nonspecific adsorption of proteins on the surface, and enables the covalent attachment of the recognition antibody. The subsequent detection of specific interaction toward antigen was monitored in real-time by SPR and confirmed by ellipsometric measurements. This lipid-based biosensing platform is versatile and can be adapted to the biorecognition reaction of interest. (C) 2015 Elsevier B.V. All rights reserved.
引用
收藏
页码:997 / 1003
页数:7
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