scholarly journals The interaction of clenbuterol hydrochloride with bovine hemoglobin using spectroscopic techniques and molecular modeling methods

2009 ◽  
Vol 23 (5-6) ◽  
pp. 271-279 ◽  
Author(s):  
Yun Wu ◽  
Hui Mao ◽  
Bo Zhao ◽  
Jian Shen
Keyword(s):  
Molecular Modeling ◽  
Protein Secondary Structure ◽  
Binding Mode ◽  
Bovine Hemoglobin ◽  
Spectroscopic Techniques ◽  
Electronic Interaction ◽  
Physiological Conditions ◽  
Modeling Methods ◽  
Clenbuterol Hydrochloride ◽  
Hoff Equation

The interaction of clenbuterol hydrochloride (CL) to bovine hemoglobin (BHb) under physiological conditions was investigated by using UV-vis absorption, fluorescence, circular dichroism (CD) and molecular modeling. The fluorescence intensity of BHb decreased regularly with the gradual increasing concentration of CL. It is observed that there was a prominent interaction between CL and BHb. The fluorescence data revealed that the fluorescence quenching is a static process, and the thermodynamic parameters were calculated according to the Van't Hoff equation. The alternations of protein secondary structure in the presence of CL were determined by the evidence of CD. Molecular modeling study that corroborate our experimental results revealed that the binding mode of CL–BHb complex could be attributed to the hydrophobic interaction and hydrogen bonding, but electronic interaction cannot be excluded.

scholarly journals Interaction of thiacloprid with bovine hemoglobin using spectroscopic and molecular modeling methods

2010 ◽  
Vol 24 (5) ◽  
pp. 559-566
Author(s):  
Chang-Yun Chen ◽  
Bo Zhao ◽  
Zheng-Wu Wang
Keyword(s):  
Hydrogen Bonding ◽  
Molecular Modeling ◽  
Protein Secondary Structure ◽  
Binding Constants ◽  
Entropy Change ◽  
Binding Mode ◽  
Cd Spectroscopy ◽  
Bovine Hemoglobin ◽  
Standard Entropy ◽  
Α Helix

The interaction of thiacloprid (TL) to bovine hemoglobin (BHb) under physiological conditions was investigated by using fluorescence spectroscopy, circular dichroism spectroscopy (CD) and molecular modeling. The fluorescence intensity of BHb decreased regularly with the gradual increasing concentration of TL. It is observed that there was a prominent interaction between TL and BHb. The binding constantsKAat 288, 298 and 308 K obtained are 8.04, 5.26 and 3.08×104l · mol–1, respectively. The standard enthalpy change (ΔH°) and the standard entropy change (ΔS°) are calculated to be –34.54 KJ · mol–1and –25.77 J · mol–1 · K–1, which indicated that hydrogen bonding forces play major role in the interaction between TL and BHb. The alternations of protein secondary structure in the presence of TL were determined by CD spectroscopy. The results revealed that the content of α-helix was decreased from 51.85% in free BHb to 48.14% in TL–BHb complex. Molecular modeling study and our experimental results both showed that the binding mode of TL–BHb complex could be attributed to hydrogen bonding and hydrophobic interaction.

scholarly journals Investigation of the mechanism of binding of thiacloprid to human serum albumin using spectroscopic techniques and molecular modeling methods

2011 ◽  
Vol 25 (2) ◽  
pp. 113-122 ◽  
Author(s):  
Chuanxian Wang ◽  
Qinghua Chu ◽  
Changyun Chen ◽  
Zhao Bo
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interactions ◽  
Entropy Change ◽  
Binding Pocket ◽  
Cd Spectroscopy ◽  
Spectroscopic Techniques ◽  
Modeling Methods

Fluorescence spectroscopy, UV absorption, circular dichroism (CD) spectroscopy and molecular modeling methods were used to characterize the binding properties of thiacloprid (TL) with human serum albumin (HSA) at molecular level under physiological conditions. The fluorescence intensity of HSA decreased regularly with the gradually increasing concentration of thiacloprid. The binding constant K at three different temperatures (290, 300 and 310 K) were 3.07, 2.74 and 1.35 × 104M−1, respectively, for TL–HSA interaction have been calculated from the relevant fluorescence data. CD spectroscopic measurements have shown that the secondary structures of the protein have been changed by the interaction of thiacloprid with HSA. Furthermore, the study of molecular modeling indicated that thiacloprid could be located on the surface of the binding pocket of subdomains IIA in HSA. The hydrophobic interaction was the major acting force and there are H-bonds and electrostatic interactions between TL and HSA, which is in good agreement with the results from the experimental thermodynamic parameters (the enthalpy change ΔH0and the entropy change ΔS0were calculated to be -20.378 kJ/mol and 16.328 J/mol K according to the Van9t Hoff equation).

scholarly journals Interaction of Irbesartan with Bovine Hemoglobin Using Spectroscopic Techniques and Molecular Docking

2012 ◽  
Vol 27 ◽  
pp. 119-128 ◽  
Author(s):  
Ai-Ping Yang ◽  
Mei-Hua Ma ◽  
Xiao-Hua Li ◽  
Mao-Yun Xue
Keyword(s):  
Hydrogen Bond ◽  
Molecular Docking ◽  
Binding Site ◽  
Binding Free Energy ◽  
Protein Secondary Structure ◽  
Cd Spectroscopy ◽  
Electrostatic Energy ◽  
Bovine Hemoglobin ◽  
Spectroscopic Techniques ◽  
Hydrogen Bond Formation

The binding of irbesartan to bovine hemoglobin (BHb) has been investigated for the first time by using UV-Vis absorption, fluorescence, circular dichroism (CD), and molecular docking. The binding site numbernand binding constantKwere calculated to be 1 and , respectively. The alternations of protein secondary structure in the presence of irbesartan was demonstrated using CD spectroscopy. Furthermore, molecular docking indicated that irbesartan could bind to the site 2 of BHb. The analysis of the binding site of irbesartan within the BHb molecule suggested that hydrophobic interaction, hydrogen bond formation, and electrostatic interaction could account for the binding of irbesartan. The hydrogen bond of irbesartan with His87 in the C chain of BHb has been formed. The electrostatic energy, van der Waals energy, and binding free energy were calculated to be −460.3, −224.2, and−684.5 kcal, respectively.

Insight into the Inhibitory Mechanism and Binding Mode Between D77 and HIV-1 Integrase by Molecular Modeling Methods

2011 ◽  
Vol 29 (2) ◽  
pp. 311-323 ◽  
Author(s):  
Ping Li ◽  
Jian Jun Tan ◽  
Ming Liu ◽  
Xiao Yi Zhang ◽  
Wei Zu Chen ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Binding Mode ◽  
Inhibitory Mechanism ◽  
Modeling Methods ◽  
Insight Into ◽  
Hiv 1

Analysis of the binding mechanism between o-phenylenediamine and bovine hemoglobin by molecular spectroscopy and molecular modeling methods

2019 ◽  
Vol 52 (10) ◽  
pp. 622-632 ◽  
Author(s):  
Jian-Li Liu ◽  
Yu-Chi Kong ◽  
Jing-Yi Miao ◽  
Yong-Lin He ◽  
Ruo-Chen Bi ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Molecular Spectroscopy ◽  
Bovine Hemoglobin ◽  
Binding Mechanism ◽  
Modeling Methods

DNase I – DNA interaction alters DNA and protein conformations

2008 ◽  
Vol 86 (3) ◽  
pp. 244-250 ◽  
Author(s):  
C.N. N’soukpoé-Kossi ◽  
S. Diamantoglou ◽  
H.A. Tajmir-Riahi
Keyword(s):  
Binding Constant ◽  
Protein Secondary Structure ◽  
Binding Mode ◽  
Dna Interaction ◽  
Minor Groove ◽  
Dnase I ◽  
Protein Conformations ◽  
Physiological Conditions ◽  
Α Helix ◽  
The Right

Human DNase I is an endonuclease that catalyzes the hydrolysis of double-stranded DNA predominantly by a single-stranded nicking mechanism under physiological conditions in the presence of divalent Mg and Ca cations. It binds to the minor groove and the backbone phosphate group and has no contact with the major groove of the right-handed DNA duplex. The aim of this study was to examine the effects of DNase I – DNA complexation on DNA and protein conformations.We monitored the interaction of DNA with DNase I under physiological conditions in the absence of Mg2+, with a constant DNA concentration (12.5 mmol/L; phosphate) and various protein concentrations (10–250 µmol/L). We used Fourier transfrom infrared, UV-visible, and circular dichroism spectroscopic methods to determine the protein binding mode, binding constant, and effects of polynucleotide–enzyme interactions on both DNA and protein conformations. Structural analyses showed major DNase–PO2 binding and minor groove interaction, with an overall binding constant, K, of 5.7 × 105 ± 0.78 × 105 (mol/L)–1. We found that the DNase I – DNA interaction altered protein secondary structure, with a major reduction in α helix and an increase in β sheet and random structures, and that a partial B-to-A DNA conformational change occurred. No DNA digestion was observed upon protein–DNA complexation.

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