A Spectroscopic and Molecular Simulation Approach toward the Binding Affinity between Lysozyme and Phenazinium Dyes: An Effect on Protein Conformation

被引：70

作者：

Millan, Sabera ^{[1
]}

Satish, Lakkoji ^{[1
]}

Bera, Krishnendu ^{[2
]}

Susrisweta, B. ^{[1
]}

Singh, Durg Vijay ^{[2
]}

Sahoo, Harekrushna ^{[1
]}

机构：

[1] Natl Inst Technol, Dept Chem, Rourkela, Odisha, India

[2] Cent Univ South Bihar, Dept Bioinformat, Patna, Bihar, India

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2017年 / 121卷 / 07期

关键词：

HUMAN SERUM-ALBUMIN; FLUORESCENCE EMISSION; CIRCULAR-DICHROISM; NEUTRAL RED; DOCKING; STABILITY; DYNAMICS; THERMODYNAMICS; EXCITATION; MECHANISM;

D O I：

10.1021/acs.jpcb.6b10991

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：

A comparative study of binding interaction between Safranin O (SO) and Neutral Red (NR) with lysozyme (Lyz) has been reported using several spectroscopic methods along with computational approaches. Steady-state fluorescence measurements revealed static quenching as the major quenching mechanism in Lyz SO and Lyz NR interaction, which is further supported by time-resolved fluorescence and UV-vis measurements. Additionally, binding and thermodynamic parameters of these interactions are calculated from temperature dependent fluorescence data. Moreover, conformational changes of protein upon binding with SO and NR are provided by synchronous and circular dichroism (CD) measurements. Molecular docking study provided the exact binding location of SO and NR. in lysozyme. Along with this study, molecular dynamics simulation is carried out to measure the stability of Lyz, Lyz SO, and Lyz NR complex. The present study revealed the strong binding affinity of dyes with lysozyme, and this study would be helpful toward medical and environmental science.

引用

页码：1475 / 1484

页数：10

共 51 条

[1] Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes [J].