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4-potential characterization of collagen and bovine serum albumin modified silica nanoparticles: a comparative study

机译:胶原蛋白和牛血清白蛋白修饰的二氧化硅纳米粒子的4位电势表征:一项比较研究

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摘要

In this study, bovine serum albumin (BSA) and collagen (COLL) were adsorbed independent of one another, onto the surface of silica nanoparticles (SNPs) at pH's where the -potential of the proteins were equal in magnitude, but opposite to the SNP surface to ascertain the differences in surface coverage and conformation in the adsorbed layer. In both systems, increasing the concentra_tion of free protein resulted in an increase in protein surface coverage and values, with values approaching that of native protein at high surface coverage. However, a lower critical charge reversal concentration range was measured for COLL relative to BSA (COLL: 0-25 μg/mL, BSA: 25_90 _g/mL). Additionally, a considerable difference in for adsorbed protein versus free protein was observed. These results when interpreted in terms of the theory of Ottewill and Watanabe indicate a higher Gibbs energy of associa_tion for COLL versus BSA on SNP surfaces, accompanied by perturbation in protein structure.
机译:在这项研究中,牛血清白蛋白(BSA)和胶原蛋白(COLL)彼此独立地吸附在pH值等于蛋白质电位但与SNP相反的pH的二氧化硅纳米颗粒(SNPs)表面上。以确定吸附层表面覆盖率和构象的差异。在这两个系统中,增加游离蛋白质的浓度会导致蛋白质表面覆盖率和值的增加,在高表面覆盖率时其值接近天然蛋白质的值。但是,相对于BSA,COLL的临界电荷逆转浓度范围较低(COLL:0-25μg/ mL,BSA:25_90_g / mL)。另外,观察到吸附蛋白与游离蛋白的显着差异。当用Ottewill和Watanabe的理论解释这些结果时,表明SNP表面上COLL与BSA的COLL与BSA具有更高的吉布斯缔合能,并伴随着蛋白质结构的扰动。

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