A comprehensive study of lysozyme adsorption using dual polarization interferometry and quartz crystal microbalance with dissipation

被引:56
作者
Xu, Kairuo [1 ]
Ouberai, Myriam M. [1 ]
Welland, Mark E. [1 ]
机构
[1] Univ Cambridge, Dept Engn, Nanosci Ctr, Cambridge CB3 0FF, England
基金
英国生物技术与生命科学研究理事会;
关键词
Protein adsorption; DPI; QCM-D; Percentage solvation; Viscoelastic property; Protein orientation; EGG-WHITE LYSOZYME; SCANNING FORCE MICROSCOPY; BOVINE SERUM-ALBUMIN; PROTEIN ADSORPTION; CONFORMATIONAL-CHANGES; ADSORBED PROTEINS; HYDROPHOBIC SURFACES; KINETICS; SILICA; RESOLUTION;
D O I
10.1016/j.biomaterials.2012.10.078
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
Protein adsorption plays a crucial role in biomaterial surface science as it is directly linked to the biocompatibility of artificial biomaterial devices. Here, elucidation of protein adsorption mechanism is effected using dual polarization interferometry and a quartz crystal microbalance to characterize lysozyme layer properties on a silica surface at different coverage values. Lysozyme is observed to adsorb from sparse monolayer to multilayer coverage. At low coverage an irreversibly adsorbed layer is formed with slight deformation consistent with side-on orientation. At higher coverage values dynamic re-orientation effects are observed which lead to monolayer surface coverages of 2-3 ng/mm(2) corresponding to edge-on or/and end-on orientations. These monolayer thickness values ranged between 3 and 4.5 nm with a protein density value of 0.60 g/mL and with 50 wt% solvent mass. Further increase of coverage results formation of a multilayer structure. Using the hydration content and other physical layer properties a tentative model lysozyme adsorption is proposed. (C) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1461 / 1470
页数:10
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