Investigation of mechanistic interactions between Rifampicin and bovine serum albumin in the presence of different surfactants

被引:2
作者
Shingda, Sampat R. [1 ]
Ali, Parvez S. [2 ]
Gandhare, Nilesh V. [3 ]
Pathan, Naziyanaz B. [4 ]
Ansari, Nizamul H. [5 ]
机构
[1] Nagpur Univ, Arvindbabu Deshmukh Mahavidyalaya, Dept Chem, RTM, Nagpur, Maharashtra, India
[2] Prince Sultan Mil Med City, Ctr Hlth Studies, Riyadh 11159, Saudi Arabia
[3] Nagpur Univ, RTM, Nabira Mahavidyalaya, Dept Chem, Katol, India
[4] Nagpur Univ, Inst Sci, RTM, Dept Chem, Nagpur, Maharashtra, India
[5] Sant Baba Bhag Singh Univ, Dept Phys Sci Chem, Jalandhar, Punjab, India
关键词
Rifampicin; bovine serum albumin; surfactants; mechanistic interactions; multispectroscopic studies; BINDING; INHIBITION; SULFATE; DESIGN; BSA;
D O I
10.1080/01932691.2021.1997759
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
Rifampicin, is an antibiotic used in the treatment of numerous types of bacterial infections, including tuberculosis, Mycobacterium avium complex, leprosy, and Legionnaires' disease. To explicate the binding interactions of Rifampicin with bovine serum albumin (BSA) at molecular level, in the presence of cationic, anionic, and neutral surfactants, it is urgent to investigate their interactions to accomplish its pharmacokinetic and pharmacodynamics gaps vital for advance development and improvement as a therapeutic drug. Thus, we have investigated the binding interaction of Rifampicin with BSA at physiological pH 7.4 in the presence and absence of surfactants Sodium dodecyl sulfate, Cetyltrimethylammonium bromide, and Tween 80. The multispectroscopic studies of Rifampicin with BSA as investigated by UV-visible, fluorescence, and circular dichroism spectroscopy shown a significant stabilization of BSA in the presence of surfactants; that can help in designing more competent drug formulations from a pharmaceutical point of view.
引用
收藏
页码:1075 / 1084
页数:10
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