Refolding of urea denatured cytochrome c: Role of hydrophobic tail of the cationic gemini surfactants
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- 作者：Rajan Patel ; rajanpatelpcy@gmail.com" class="auth_mail" title="E-mail the corresponding author ; rpatel@jmi.ac.in" class="auth_mail" title="E-mail the corresponding author ; Muzaffar Ul Hassan Mir ; Upendra Kumar Singh ; Ilyas Beg ; Asimul Islam ; Abbul Bashar Khan
- 关键词：Horse heart cytochrome c ; Protein folding ; Molten globule-like state ; Hydrophobic interactions ; Cationic gemini surfactants
- 刊名：Journal of Colloid and Interface Science
- 出版年：2016
- 出版时间：15 December 2016
- 年：2016
- 卷：484
- 期：Complete
- 页码：205-212
- 全文大小：1720 K
文摘
The refolding of urea denatured horse heart cytochrome c (h-cyt-c) under the influence of ester based cationic gemini surfactants [ethane-1, 2-diyl bis(N, N-dimethyl-N-alkylammoniumacetoxy) dichlorides] 16-E2-16, 14-E2-14 and 12-E2-12 (n-E2-n) was performed by using UV–visible, fluorescence and circular dichroism (CD) spectroscopic techniques. We found that n-E2-n geminis promote the formation of molten globule (MG) like state upon addition into the urea denatured h-cyt-c. The comparative study of refolding of denatured h-cyt-c with n-E2-n, cationic gemini surfactant show stabilization of MG-like state influenced by hydrophobic interactions. The formation of MG-like state from the unfolded protein confirms the presence of some regular structures induced by n-E2-n gemini surfactants. Thermodynamic parameters for refolding of h-cyt-c by n-E2-n were also measured and the m-values of all the refolded states of h-cyt-c by n-E2-n show marked difference. The higher m-values correspond to the larger hydrophobic chain length indicates that refolding ability of the n-E2-n depends on the alkyl chain length. The result is related to the stronger hydrophobic forces due to the presence of two head groups and two hydrophobic hydrocarbon tails. This study showed that these cationic gemini surfactants were efficiently utilized in the protein refolding studies.