Quenching interaction of BSA with DTAB is dynamic in nature: A spectroscopic insight

被引：24

作者：

Das, Nirmal Kumar ^{[1
]}

Pawar, Lavanya ^{[1
]}

Kumar, Naveen ^{[1
]}

Mukherjee, Saptarshi ^{[1
]}

机构：

[1] Indian Inst Sci Educ & Res Bhopal, Dept Chem, Bhopal 462066, Madhya Pradesh, India

来源：

CHEMICAL PHYSICS LETTERS | 2015年 / 635卷

关键词：

BOVINE SERUM-ALBUMIN; SODIUM DODECYL-SULFATE; IONIC SURFACTANTS; CATIONIC SURFACTANTS; GLOBULAR-PROTEINS; FLUORESCENCE; BINDING; STATE; PH; SCATTERING;

D O I：

10.1016/j.cplett.2015.06.033

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The role of electrostatic interactions between the protein, Bovine Serum Albumin (BSA) and the cationic surfactant, dodecyltrimethylammonium bromide (DTAB) has been substantiated using spectroscopic approaches. The primary mechanism of fluorescence quenching of the tryptophan of BSA is most probably dynamic in nature as the complex formation resulting in a protein-surfactant assembly is not very spontaneous. The weak interaction buries the tryptophan amino acid residue inside the protein scaffolds which have been quantitatively proved by our acrylamide quenching studies. The loss in the secondary structure of the protein as a result of interaction with DTAB has been elucidated by CD spectroscopy. (C) 2015 Elsevier B.V. All rights reserved.

引用

页码：50 / 55

页数：6

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