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首页> 外文期刊>Journal of the American Chemical Society >MACROMOLECULAR COMPLEXATION BETWEEN BOVINE SERUM ALBUMIN AND THE SELF-ASSEMBLED HYDROGEL NANOPARTICLE OF HYDROPHOBIZED POLYSACCHARIDES
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MACROMOLECULAR COMPLEXATION BETWEEN BOVINE SERUM ALBUMIN AND THE SELF-ASSEMBLED HYDROGEL NANOPARTICLE OF HYDROPHOBIZED POLYSACCHARIDES

机译：牛血清白蛋白与加氢多糖的自组装水合纳米粒子之间的大分子复杂化

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摘要

Macromolecular complexation between bovine serum albumin (BSA) and self-assembled hydrogel nanoparticle formed by the self-ag,gregation of cholesterol-bearing pullulan (CHP) was studied by high performance size exclusion column chromatography (HPSEC) and circular dichroism (CD). The CHP self-aggregates complexed with one BSA molecule to give colloidally stable nanoparticles (R(G) = 17 nm) at pH 7.0 and 25 degrees C. This was almost irrespective of the substitution degree of the cholesterol group of CHP. The helical content of BSA decreased upon complexation. Unfolding of BSA by either heating or a denaturant such as urea was largely suppressed upon complexation. BSA would be incorporated inside into the hydrogel matrix of the CHP nanoparticle. Kinetic analysis of the complexation suggested a two-step process: namely, the fast pre-equilibrium of looser binding of BSA to the CHP self-aggregate followed by the slower process of tighter inclusion into the hydrogel network. The substitution degree of the cholesterol group in CHP significantly affected the complexation kinetics.
机译：通过高效排阻色谱法（HPSEC）和圆二色性（CD）研究了牛血清白蛋白（BSA）与自组装的，含胆固醇的支链淀粉（CHP）的聚集形成的自组装水凝胶纳米颗粒之间的大分子复合。 CHP与一个BSA分子复合形成的自聚集体，在pH 7.0和25摄氏度下产生胶体稳定的纳米颗粒（R（G）= 17 nm）。这几乎与CHP胆固醇基团的取代度无关。络合后，BSA的螺旋含量降低。络合后，通过加热或变性剂（例如尿素）使BSA的解开得到很大程度的抑制。 BSA将被并入CHP纳米颗粒的水凝胶基质内部。络合的动力学分析表明，该过程分为两个步骤：即，BSA与CHP自聚集体较松散结合的快速预平衡，然后是紧密结合到水凝胶网络中的较慢过程。 CHP中胆固醇基团的取代度显着影响络合动力学。

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