Dynamic alterations of fibronectin layers on copolymer substrates with graded physicochemical characteristics.
Dynamic alterations of fibronectin layers on copolymer substrates with graded physicochemical characteristics.
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具有分级理化特性的共聚物基底上纤连蛋白层的动态变化。
DOI：
10.1021/la0362627
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发表时间：
2004
期刊：
影响因子：
--
通讯作者：
C. Werner
中科院分区：
文献类型：
--
作者：
L. Renner;T. Pompe;K. Salchert;C. Werner
根据马来酸共聚物膜的物化特性，研究了纤维粘连蛋白在纯缓冲液和人血清白蛋白或纤维粘连蛋白溶液中的解吸和交换。尽管纤维连接蛋白的预吸附量只有很小的差别，但与更亲水和带负电荷的聚合物表面相比，蛋白质在疏水性更强的聚合物表面表现出显著的锚定作用。纤维连接蛋白最有效地交换预吸附层(即，在同位移过程中)，而纯缓冲液和人血清白蛋白溶液诱导纤维连接蛋白的解吸或交换程度较低或相似。在置换实验中，由于纤维连接蛋白或人血清白蛋白的额外吸附，蛋白质的总吸附量增加，并伴随着预吸附的纤维连接蛋白的部分交换。对纤维连接蛋白在任何一种底物上的解吸和交换动力学的评价表明，有两种表面附着的蛋白质群体--一种快速解吸物种和一种缓慢解吸和交换速率物种。通过多元回归分析，证实了聚合物底物的表面特征决定了蛋白质的解吸和交换程度，而蛋白质层变化的动力学仅取决于蛋白质的扩散行为。
Desorption and exchange of preadsorbed fibronectin layers in pure buffer solution and solutions of human serum albumin or fibronectin, respectively, were studied in dependence on the physicochemical characteristics of maleic acid copolymer films used as substrates. Although the preadsorbed amount of fibronectin differed only slightly, the protein was found to exhibit a significantly enhanced anchorage at the more hydrophobic polymer surface as compared to the more hydrophilic and more negatively charged polymer surface. The preadsorbed fibronectin layer was most efficiently exchanged by fibronectin (i.e., in the homodisplacement process) while pure buffer solution and human serum albumin solutions induced desorption or exchange of fibronectin to lower and similar degrees. An increase of the total adsorbed amount of protein due to additional adsorption of fibronectin or human serum albumin accompanied the partial exchange of the preadsorbed fibronectin in the displacement experiments. Evaluation of the kinetics of desorption and exchange of fibronectin at any of the substrates revealed two kinds of surface-attached protein populations--a fast desorbing species and a species with a slow desorption and exchange rate. By a multivariate regression analysis the surface characteristics of the polymer substrate were confirmed to determine the degree of protein desorption and exchange while the dynamics of the layer alteration was found to solely depend on the diffusion behavior of the proteins.