کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1200651 | 1493606 | 2013 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: A novel nickel-chelated surfactant for affinity-based aqueous two-phase micellar extraction of histidine-rich protein A novel nickel-chelated surfactant for affinity-based aqueous two-phase micellar extraction of histidine-rich protein](/preview/png/1200651.png)
• Nickel-chelated surfactant was prepared by modifications of Triton X-114.
• Nickel-chelated surfactant insertion inhibited micellization and micellar growth.
• Partition coefficient of his-tagged protein was over 20 times enhanced.
• Nickel-chelated micellar system exhibited high affinity for histidine-rich protein.
Aqueous two-phase micellar systems (ATPMSs) composed of nonionic surfactants are considered promising for the separation and purification of proteins. To improve the specificity of ATPMSs, a novel nickel-chelated surfactant was prepared by successive modifications of Triton X-114 (TX). Characterizations by Fourier transformation infrared spectroscopy demonstrated the successful synthesis of the nickel-chelated surfactant (TX-Ni). The cloud point, critical micelle concentration (CMC), molecular interaction parameter and micelle size were measured for the mixed surfactant system of TX-Ni and TX to achieve a full understanding of their aggregation behaviors. The results showed that mixed micelles were formed, and the cloud point increased with the mole fraction of TX-Ni because TX-Ni had a more hydrophilic head group than TX. Moreover, the reduction of micelle size revealed by light scattering experiments indicated that the insertion of TX-Ni inhibited the micellar growth due to the increased steric and electrostatic repulsion. Finally, the efficiency of TX-Ni as an affinity surfactant was demonstrated by the affinity partitioning of histidine-tagged enhanced green fluorescent protein with an over 20-fold increase of the partition coefficient (from 0.60 to 12.42). This affinity-based ATPMS is thus considered promising for providing a versatile platform for the separation of histidine-rich proteins.
Journal: Journal of Chromatography A - Volume 1320, 13 December 2013, Pages 118–124