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Gemini表面活性剂与蛋白质的相互作用:pH值、温度及表面活性剂立体化学的影响

Gemini surfactant-protein interactions: effect of pH, temperature, and surfactant stereochemistry.

作者信息

Faustino Célia M C, Calado António R T, Garcia-Rio Luís

机构信息

iMed.UL, Faculty of Pharmacy, University of Lisbon, Av. Prof. Gama Pinto, 1649-003 Lisboa, Portugal.

出版信息

Biomacromolecules. 2009 Sep 14;10(9):2508-14. doi: 10.1021/bm9004723.

Abstract

The interactions between bovine serum albumin (BSA) and gemini surfactants derived from cystine have been investigated and were compared with the conventional single-chain surfactant derived from cysteine. The influence of the stereochemistry of the gemini surfactant on its behavior toward BSA was also investigated, as well as the effects of pH and temperature. Electrical conductivity and surface tension measurements were used to obtain important system parameters such as critical aggregation concentration (cac), polymer saturation point (psp), degree of ionization (alpha), and the amount of surfactant binding to protein (M). Stereochemistry was found to influence the surface properties of the surfactants studied and their interaction with BSA but not their micellar properties in solution.

摘要

已对牛血清白蛋白(BSA)与源自胱氨酸的双子表面活性剂之间的相互作用进行了研究,并与源自半胱氨酸的传统单链表面活性剂进行了比较。还研究了双子表面活性剂的立体化学对其与BSA行为的影响,以及pH值和温度的影响。通过电导率和表面张力测量来获得重要的系统参数,如临界聚集浓度(cac)、聚合物饱和点(psp)、电离度(α)以及与蛋白质结合的表面活性剂的量(M)。发现立体化学会影响所研究表面活性剂的表面性质及其与BSA的相互作用,但不会影响其在溶液中的胶束性质。

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