Molecular docking and experimental investigation of new indole derivative cyclooxygenase inhibitor to probe its binding mechanism with bovine serum albumin

被引：53
作者：
Wani, Tanveer A. [1 ]
Bakheit, Ahmed H. [1 ,2 ]
Zargar, Seema [3 ]
Bhat, Mashooq A. [1 ]
Al-Majed, Abdulrahman A. [1 ]
机构：
[1] King Saud Univ, Coll Pharm, Dept Pharmaceut Chem, POB 2457, Riyadh 11451, Saudi Arabia
[2] Al Neelain Univ, Fac Sci & Technol, Dept Chem, Khartoum, Sudan
[3] King Saud Univ, Coll Sci, Dept Biochem, POB 22452, Riyadh 11451, Saudi Arabia
来源：
BIOORGANIC CHEMISTRY | 2019年 / 89卷
关键词：
N-ALKYL SULFATES; BETA-LACTOGLOBULIN; HOLO-TRANSFERRIN; ANTICANCER DRUG; ACID; THERMODYNAMICS; INTERMEDIATE; BEHAVIOR; HTF; HSA;
D O I：
10.1016/j.bioorg.2019.103010
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The indole derivative 2-(5-methoxy-2-methyl-1H-indol-3-yl)-N'-[(E)-(3-nitrophenyl) methylidene]acetohydrazide (IND) was synthesized for its therapeutic potential to inhibit cyclooxygenase (COX)-II. Binding if IND to bovine serum albumin (BSA) was investigated was because most drugs bind to serum albumin in-vivo. Fluorescence, UV-vis spectrophotometry and molecular modeling methodologies were employed for studying the interaction mechanism. The intrinsic fluorescence of BSA was quenched by BSA and the quenching mechanism involved was static quenching. The binding constants between IND and BSA at the three studied temperatures (298, 301 and 306 K) were 1.09 x 10(5), 4.36 x 10(4) and 1.23 x 10(4 )L mol(-1) respectively. The most likely site for binding IND to BSA was Site I (subdomain IIA). The analysis of thermodynamic parameter revealed the involvement of hydrogen bonding and van der Waals forces in the IND-BSA interaction. Synchronous fluorescence spectroscopic (SFS) and UV-vis spectrophotometric studies suggested conformational change in BSA molecule post interaction to IND. Molecular docking and the experimental results corroborated one another. The study can prove as an insight for future IND drug development.
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页数：7
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