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Adsorption Kinetics Conformation and Mobility of the Growth Hormone and Lysozyme on Solid Surfaces Studied with TIRF

机译:用TIRF研究固体表面上生长激素和溶菌酶的吸附动力学形态和流动性

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摘要

Interactions of recombinant human growth hormone and lysozyme with solid surfaces are studied using total internal reflection fluorescence (TIRF) and monitoring the protein’s intrinsic tryptophan fluorescence. The intensity, spectra, quenching, and polarization of the fluorescence emitted by the adsorbed proteins are monitored and related to adsorption kinetics, protein conformation, and fluorophore rotational mobility. To study the influence of electrostatic and hydrophobic interactions on the adsorption process, three sorbent surfaces are used which differ in charge and hydrophobicity. The chemical surface groups are silanol, methyl, and quaternary amine. Results indicate that adsorption of hGH is dominated by hydrophobic interactions. Lysozyme adsoption is strongly affected by the ionic strength. This effect is probably caused by an ionic strength dependent conformational state in solution which, in turn, influences the affinity for adsorption. Both proteins are more strongly bound to hydrophobic surfaces and this strong interaction is accompanied by a less compact conformation. Furthermore, it was seen that regardless of the characteristics of the sorbent surface, the rotational mobility of both proteins’ tryptophans is largely reduced upon adsorption.
机译:利用全内反射荧光(TIRF)并监测蛋白质的固有色氨酸荧光,研究了重组人生长激素和溶菌酶与固体表面的相互作用。监测被吸附蛋白发射的荧光的强度,光谱,猝灭和极化,并与吸附动力学,蛋白构象和荧光团旋转迁移率相关。为了研究静电和疏水相互作用对吸附过程的影响,使用了三个电荷和疏水性不同的吸附剂表面。化学表面基团是硅烷醇,甲基和季胺。结果表明,hGH的吸附主要是疏水相互作用。溶菌酶的吸附受到离子强度的强烈影响。这种影响可能是由于溶液中依赖离子强度的构象状态引起的,进而影响了吸附的亲和力。两种蛋白都更牢固地结合到疏水表面,并且这种强相互作用伴随着不太紧密的构象。此外,可以看出,不管吸附剂表面的特性如何,两种蛋白质的色氨酸在吸附时的旋转迁移率都大大降低了。

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