Interaction of NAEn-s-n gemini surfactants with bovine serum albumin: A structure-activity probe

被引:42
作者
Wang, Houchen [1 ]
Jiang, Xiaohui [1 ]
Zhou, Limei [1 ]
Cheng, Zhenjun [1 ]
Yin, Wenmin [1 ]
Duan, Ming [2 ]
Liu, Pingli [2 ]
Jiang, Xiaomin [3 ]
机构
[1] China W Normal Univ, Chem Synth & Pollut Control Key Lab Sichuan Prov, Nanchong 637009, Sichuan, Peoples R China
[2] SW Petr Univ, State Key Lab Oil & Gas Reservoir Geol & Exploita, Chengdu 610500, Sichuan, Peoples R China
[3] SW Elect Power Design Inst, Chengdu 61002, Sichuan, Peoples R China
基金
中国国家自然科学基金;
关键词
Bovine serum albumin; Cationic gemini surfactant; Fluorescence quenching; Attenuated total reflection FTIR (ATR-FTIR); SYNCHRONOUS FLUORESCENCE DETERMINATION; ANGLE NEUTRON-SCATTERING; CATIONIC SURFACTANTS; VESICLE FORMATION; PROTEIN; BEHAVIOR; SPACER; LIPIDS; CHAIN; AGGREGATION;
D O I
10.1016/j.jlumin.2012.08.058
中图分类号
O43 [光学];
学科分类号
070207 ; 0803 ;
摘要
Gemini surfactants, alpha-omega-bis (3-(alkyloxylacyl) pyridinium) propane/butane/hexane dibromide (designated as NAEn-s-n), have been prepared and the interactions of NAEn-s-n with bovine serum albumin (BSA) were investigated by fluorescence, UV-vis and FTIR spectroscopies. The intrinsic fluorescence of BSA was significantly quenched by NAEn-s-n through static quenching. NAEn-s-n combined mainly with Trp-212 in BSA by van der Waals force, hydrogen bonding, electrostatic and hydrophobic interaction. The binding process was spontaneous, exothermic and enthalpy driven. The synchronous and tridimensional fluorescence revealed the changed conformation of the peptide backbone and the altered microenvironment of tryptophan and tyrosine residues in BSA. The red-shift in the IR spectrum of the BSA amide I peak, the blue-shift of amide II peak, as well as the appearance of a new peak at around 1514 cm(-1) suggested unfolding of the protein secondary structure upon the addition of NAEn-s-n. The lengths of spacer and hydrophobic chain greatly influenced the interaction. With the lengthening alkyl chain in NAEn-s-n, the binding constant of BSA-NAEn-4-n increased, while the thermodynamic parameters and the a-helix content of BSA decreased. This indicated an enhancement of hydrophobic interaction between BSA and NAEn-s-n. However, these values (i.d. binding constant, alpha-helix content etc.) fluctuated with methylene numbers in the spacer of NAEn-s-n, which might be due to the different spatial arrangement of the spacer of the gemini surfactants. This investigation may shed new light on the understanding of structure-activity correlation. (c) 2012 Elsevier B.V. All rights reserved.
引用
收藏
页码:138 / 147
页数:10
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