Spectroscopic Investigations of the Binding Interaction of a New Indanedione Derivative with Human and Bovine Serum Albumins

Stan, Dana; Matei, Iulia; Mihailescu, Carmen-Marinela; Savin, Mihaela; Hillebrand, Mihaela; Baciu, I; Matache, Mihaela

doi:10.3390/molecules14041614

Cited by 35 publications

(12 citation statements)

References 39 publications

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“…CD measurement is an important method to study the conformational changes of protein induced by small molecule. MRE is always used for expressing the alterations of protein secondary structure , which can be calculated according to the following equation:

MRE = \frac{Observed CD (italicmedg)}{10 C \cdot n \cdot l}

where C is the molar concentration of the protein. n is the number of amino acid residues (583 for BSA).…”

Section: Resultsmentioning

confidence: 99%

A combined spectroscopic and molecular docking approach to characterize binding interaction of megestrol acetate with bovine serum albumin

2014

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The binding interactions between megestrol acetate (MA) and bovine serum albumin (BSA) under simulated physiological conditions (pH 7.4) were investigated by fluorescence spectroscopy, circular dichroism and molecular modeling. The results revealed that the intrinsic fluorescence of BSA was quenched by MA due to formation of the MA-BSA complex, which was rationalized in terms of a static quenching procedure. The binding constant (Kb ) and number of binding sites (n) for MA binding to BSA were 2.8 × 10(5) L/mol at 310 K and about 1 respectively. However, the binding of MA with BSA was a spontaneous process due to the negative ∆G(0) in the binding process. The enthalpy change (∆H(0) ) and entropy change (∆S(0) ) were - 124.0 kJ/mol and -295.6 J/mol per K, respectively, indicating that the major interaction forces in the binding process of MA with BSA were van der Waals forces and hydrogen bonding. Based on the results of spectroscopic and molecular docking experiments, it can be deduced that MA inserts into the hydrophobic pocket located in subdomain IIIA (site II) of BSA. The binding of MA to BSA leads to a slight change in conformation of BSA but the BSA retained its secondary structure, while conformation of the MA has significant change after forming MA-BSA complex, suggesting that flexibility of the MA molecule supports the binding interaction of BSA with MA.

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MRE = \frac{Observed CD (italicmedg)}{10 C \cdot n \cdot l}

where C is the molar concentration of the protein. n is the number of amino acid residues (583 for BSA).…”

Section: Resultsmentioning

confidence: 99%

A combined spectroscopic and molecular docking approach to characterize binding interaction of megestrol acetate with bovine serum albumin

2014

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“…In this study, our aim was to investigate the binding mechanism of CBH with HSA and to gain deeper insight into the interaction mechanism. The combination of UV-VIS [19], fluorescence [20,21] and circular dichroism (CD) [22,23] spectroscopy, along with in silico approaches, thoroughly describe the structural alterations within HSA after binding to CBH. Further valuable information about the binding mode, binding mechanism, binding constants, and structural changes within the HSA-CBH complex are also widely explored.…”

Section: Introductionmentioning

confidence: 99%

Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and In Silico Approaches

Baig

Rahman

Rabbani

et al. 2019

IJMS

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Cyclobenzaprine hydrochloride (CBH) is a well-known muscle relaxant that is widely used to relieve muscle spasms and other pain associated with acute musculoskeletal conditions. In this study, we elucidated the binding characteristics of this muscle relaxant to human serum albumin (HSA). From a pharmaceutical and biochemical viewpoint, insight into the structure, functions, dynamics, and features of HSA-CBH complex holds great importance. The binding of CBH with this major circulatory transport protein was studied using a combination of biophysical approaches such as UV-VIS absorption, fluorescence quenching, and circular dichroism (CD) spectroscopy. Various in silico techniques, molecular docking and molecular dynamics, were also used to gain deeper insight into the binding. A reduction in the fluorescence intensities of HSA-CBH complex with a constant increase in temperature, revealed the static mode of protein fluorescence quenching upon CBH addition, which confirmed the formation of the HSA-CBH ground state complex. The alteration in the UV-VIS and far-UV CD spectrum indicated changes in both secondary and tertiary structures of HSA upon binding of CBH, further proving CBH binding to HSA. The analysis of thermodynamic parameters ∆H° and ∆S° showed that binding of CBH to HSA was dominated by intermolecular hydrophobic forces. The results of the molecular docking and molecular dynamics simulation studies also confirmed the stability of the complex and supported the experimental results.

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“…Synchronous fluorescence measurements provide information about polarity changes in the microenvironment around the fluorophores . When the wavelength interval (Δλ) is fixed at 15 or 60 nm, the synchronous fluorescence of Cu/ZnSOD is characteristic of tyrosine or tryptophan residues, respectively .…”

Section: Resultsmentioning

confidence: 99%

Probing the interactions between carboxylated multi‐walled carbon nanotubes and copper–zinc superoxide dismutase at a molecular level

Guan

Liu

Cai³

et al. 2014

Luminescence

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In order to evaluate the toxicity of multi-walled carbon nanotubes (MWCNTs-COOH) at a molecular level, the effect of MWCNTs-COOH on antioxidant enzyme copper-zinc superoxide dismutase (Cu/ZnSOD) was investigated using fluorescence spectroscopy, UV/vis absorption spectroscopy, circular dichroism (CD) spectroscopy and isothermal titration calorimetry (ITC). By deducting the inner filter effect (IFE), the fluorescence emission spectra and synchronous fluorescence spectra indicated that there were interactions between MWCNTs-COOH and Cu/ZnSOD. Moreover, the microenvironment of the amino acid residues in the enzyme was changed slightly. The UV/vis absorption and CD spectroscopic results showed appreciable conformational changes in Cu/ZnSOD. However, the results of a Cu/ZnSOD activity determination did not show any significant difference. In other words, MWCNTs-COOH has no significant effect on enzyme activity. The ITC results showed that the binding of MWCNTs-COOH to Cu/ZnSOD was a weak endothermic process, indicating that the predominant force of the binding was hydrophobic interaction. Moreover, it was essential to consider the IFE in fluorescence assays, which might affect the accuracy and precision of the results. The above results are helpful in evaluating the oxidative stress induced by MWCNTs-COOH in vivo.

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Spectroscopic Investigations of the Binding Interaction of a New Indanedione Derivative with Human and Bovine Serum Albumins

Cited by 35 publications

References 39 publications

A combined spectroscopic and molecular docking approach to characterize binding interaction of megestrol acetate with bovine serum albumin

A combined spectroscopic and molecular docking approach to characterize binding interaction of megestrol acetate with bovine serum albumin

Multi-Spectroscopic Characterization of Human Serum Albumin Binding with Cyclobenzaprine Hydrochloride: Insights from Biophysical and In Silico Approaches

Probing the interactions between carboxylated multi‐walled carbon nanotubes and copper–zinc superoxide dismutase at a molecular level

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