King Saud University, Department of Food Science and Nutrition, Faculty of Food and Agricultural Sciences, 2460 Riyadh, Saudi Arabia-11451.
King Saud University, Protein Research Chair, Department of Biochemistry, College of Science, Riyadh 11451, Saudi Arabia.
Spectrochim Acta A Mol Biomol Spectrosc. 2019 Aug 5;219:313-318. doi: 10.1016/j.saa.2019.04.062. Epub 2019 Apr 24.
The interactions between cetyltrimethylammonium bromide (CTAB) and hen egg white lysozymes (HEWL) was carried out to investigate protein-surfactant interaction mechanisms while both exist in the overall same charged state. The interactions between CTAB and the HEWL were examined with circular dichroism (CD), dynamic light scattering (DLS), fluorescence spectroscopy, and computational docking at a pH9.0 at room temperature. The far-UV CD and fluorescence results revealed that CTAB at concentrations from 0.15 to 10.0mM influenced the secondary as well as the tertiary structure of HEWL. The secondary structure of the HEWL was retained, while the tertiary structure of the HEWL was disrupted in the CTAB-treated samples at pH9.0. The hydrodynamic radii of the HEWL were also expanded in the presence of CTAB. Molecular docking studies showed that CTAB formed one electrostatic and four hydrophobic interactions, as well as one carbon hydrogen bond with HEWL. The data obtained from spectroscopic and computational studies demonstrated that the positively charged head and 18‑carbon alkyl chain of the CTAB interacted through weak electrostatic and strong hydrophobic interactions.
十六烷基三甲基溴化铵（CTAB）与鸡卵清白溶菌酶（HEWL）的相互作用，研究了在整体带相同电荷状态下，蛋白质-表面活性剂相互作用的机制。在 pH9.0 室温下，通过圆二色性（CD）、动态光散射（DLS）、荧光光谱和计算对接，研究了 CTAB 与 HEWL 之间的相互作用。远紫外 CD 和荧光结果表明，浓度从 0.15 到 10.0mM 的 CTAB 影响了 HEWL 的二级和三级结构。HEWL 的二级结构得以保留，而在 pH9.0 的 CTAB 处理样品中，HEWL 的三级结构被破坏。HEWL 的流体力学半径也在 CTAB 的存在下扩大。分子对接研究表明，CTAB 与 HEWL 形成一个静电和四个疏水相互作用，以及一个碳氢键。光谱和计算研究获得的数据表明，CTAB 的带正电荷的头部和 18 个碳烷基链通过弱静电和强疏水相互作用相互作用。
