Feiler Adam A, Sahlholm Anna, Sandberg Tomas, Caldwell Karin D
Department of Physical and Analytical Chemistry, Surface Biotechnology, Box 577, BMC, Uppsala University, SE-75123 Uppsala, Sweden.
J Colloid Interface Sci. 2007 Nov 15;315(2):475-81. doi: 10.1016/j.jcis.2007.07.029. Epub 2007 Jul 19.
The adsorption profile and viscoelastic properties of bovine submaxillary gland mucin (BSM) and bovine serum albumin (BSA), extracted from a commercial mucin preparation, adsorbing to polystyrene surfaces has been studied using quartz crystal microbalance with dissipation monitoring (QCM-D). A significant difference in the adsorption properties of the different proteins was detected; with the BSA adsorbing in a flat rigid layer whilst the mucin adsorbed in a diffuse, highly viscoelastic layer. Subsequent addition of BSA to the preadsorbed mucin layer resulted in stiffening of the protein layer which was attributed to complexation of the mucin by BSA. In contrast, a preadsorbed layer of BSA prevented mucin adsorption altogether. Combined mixtures of mucin and BSA in well defined ratios revealed intermediate properties between the two separate protein species which varied systematically with the protein ratios. The results shed light on the synergistic effects of complexation of lower molecular weight biomolecular species with mucin. The possibility to selectively control protein uptake and tailor the physical properties of the adsorbed layer makes mucin an attractive option for application in biomaterial coatings.
利用带耗散监测的石英晶体微天平（QCM-D），研究了从一种商业粘蛋白制剂中提取的牛颌下腺粘蛋白（BSM）和牛血清白蛋白（BSA）在聚苯乙烯表面的吸附情况及粘弹性特性。检测到不同蛋白质的吸附特性存在显著差异；BSA以扁平刚性层形式吸附，而粘蛋白以扩散的高粘弹性层形式吸附。随后向预吸附的粘蛋白层中添加BSA会导致蛋白质层变硬，这归因于BSA与粘蛋白的络合。相比之下，预吸附的BSA层完全阻止了粘蛋白的吸附。以明确比例混合的粘蛋白和BSA混合物显示出介于两种单独蛋白质之间的中间特性，且随蛋白质比例而系统变化。这些结果揭示了低分子量生物分子物种与粘蛋白络合的协同效应。选择性控制蛋白质吸附并定制吸附层物理性质的可能性，使粘蛋白成为生物材料涂层应用的一个有吸引力的选择。
