Probing the binding of two 19‐nortestosterone derivatives to human serum albumin: insights into the interactions of steroid hormone drugs with functional biomacromolecule

He, Jiawei; Wang, Qing; Ma, Xiaodong; Yang, Hongqin; Li, Shanshan; Xu, Kailin; Li, Hui

doi:10.1002/jmr.2540

Cited by 10 publications

(6 citation statements)

References 41 publications

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“…Dansyl-L-arginine on the FA7 site of HSA also preferentially binds to site I, whereas dansyl-L-sarcosine on FA1 binds to site III (heme-binding site) 22 . With these probes, the displacement of CR to HSA on percentage can be determined as follows 39 :where F and F 0 are the fluorescence intensities of the CR–HSA complex in absent and present of site probe, respectively. The sketch of F/F 0 against different probe concentrations was fitted as shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Computational and spectroscopic analysis of interaction between food colorant citrus red 2 and human serum albumin

Wang

Liu

et al. 2019

Sci Rep

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The main aim of this work was to gain insight into the binding properties between a food colorant, citrus red 2 (CR), and human serum albumin (HSA), which is the predominant protein in blood plasma. Here, computer simulations and multiple spectroscopies were applied to predict and characterize the interaction between CR and HSA. Docking and molecular dynamics presented a stable binding configuration with low fluctuations. Fluorescence spectroscopy and lifetime results suggested that the CR–HSA combination undergoes static quenching mechanism with binding constant of 105 L/mol. Displacement analysis showed the binding of CR at site I of HSA, which agrees with the docking results. The binding process occured spontaneously and was mainly driven by electrostatic interactions. Synchronous fluorescence and circular dichroism measurements demonstrate the changes in the microenvironment residues and α-helix contents of HSA induced by CR. The computational and experimental techniques are complementary to clearly understand the food colorant transportation and bioaccumulative toxicity in the human body.

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Section: Resultsmentioning

confidence: 99%

Computational and spectroscopic analysis of interaction between food colorant citrus red 2 and human serum albumin

Wang

Liu

et al. 2019

Sci Rep

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“…If ΔH° > 0 and ΔS° > 0, these imply that hydrophobic interactions is dominant. If ΔH° < 0 and ΔS° > 0, these imply that electrostatic interactions are predominant . The thermodynamic parameters were constant for subjected temperatures.…”

Section: Resultsmentioning

confidence: 99%

“…10,29,30 The binding forces between a biological macromole- ΔH°< 0 and ΔS°> 0, these imply that electrostatic interactions are predominant. [31][32][33] The thermodynamic parameters were constant for subjected temperatures. The changes in enthalpy (ΔH), entropy (ΔS), and free energy (ΔG) were calculated for interaction between the BLC and pioglitazone using the Van't Hoff and following Equations 6 to 8:…”

Section: Determination Of Binding Parameters and Binding Forcesmentioning

confidence: 99%

Activation of catalase by pioglitazone: Multiple spectroscopic methods combined with molecular docking studies

Yekta

Dehghan

Rashtbari

et al. 2017

J of Molecular Recognition

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Pioglitazone is an important prescription antidiabetic drug with positive roles in controlling high blood sugar in patients with type 2 diabetes. In the present study, we investigated the effects of pioglitazone on the structure and function of bovine liver catalase (BLC) using different spectroscopic and theoretical methods. UV-Vis absorption, fluorescence spectroscopy, synchronous fluorescence, and circular dichroism studies revealed conformational changes in the BLC structure and heme group in the presence of different concentrations of pioglitazone. Kinetic studies indicated that pioglitazone can increase BLC activity by approximately threefold compared with free enzyme. The fluorescence quenching data showed one binding site for pioglitazone, and the binding constants at 298, 304, and 310 K were calculated as 5.01 × 10 M , 5.8 × 10 M , and 6.6 × 10 M , respectively. The static type of quenching mechanism was mainly involved in the quenching of intrinsic emission of the enzyme. Thermodynamic data suggested that hydrophobic interactions played a major role in the binding reaction of pioglitazone with BLC. The molecular docking studies indicated that pioglitazone interacts with the cavity in the middle of the β-barrel and wrapping domain of BLC. Thus, pioglitazone can increase catalase activity by changing the BLC structure.

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“…The intrinsic fluorescence of proteins can provide information about their structure and dynamics. Therefore, Fluorescence methods have been widely used to investigate the interaction between ligands and proteins . Figure shows the fluorescence emission spectra of pepsin and trypsin with different TF concentrations.…”

Section: Resultsmentioning

confidence: 99%

“…Fluorescence quenching processes in solution are usually divided into 2 general types, namely, static quenching and dynamic quenching . To confirm the possible quenching mechanism, Stern‐Volmer equation was utilized to calculate the data at different temperatures:

\frac{F_{0}}{F} = 1 + K_{SV} ([],, Q) = 1 + K_{q} \cdot τ_{0} ([],, Q)

where F 0 and F are the fluorescence intensities of pepsin and trypsin in the absence and presence of TF, respectively.…”

Section: Resultsmentioning

confidence: 99%

Investigation and comparison of the binding between tolvaptan and pepsin and trypsin: Multi‐spectroscopic approaches and molecular docking

Huang

et al. 2016

J of Molecular Recognition

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Tolvaptan (TF), a selective arginine vasopressin V2 receptor antagonist, was approved by the Food and Drug Administration in 2009. This study mainly investigated the differences between the binding of TF with pepsin and trypsin by using a series of spectroscopy and molecular modeling methods. Thermodynamic parameters and molecular docking results suggested that the binding of TF to pepsin and trypsin were both spontaneous but driven by different forces. For pepsin, the binding was driven by hydrogen bonds and van der Waals forces; but for trypsin, it was driven by electrostatic forces and hydrophobic forces. The quenching mechanism between TF and pepsin and trypsin was investigated by fluorescence experiments and time-resolved fluorescence spectroscopy. Synchronous fluorescence and 3-dimensional fluorescence were used to investigate the micro-environmental and conformational changes of pepsin and trypsin after the insertion of TF. In addition, activity-measurement results showed that both the pepsin and trypsin activities increased with increasing TF concentration, which may help to understand the possible effect of TF on the digestion and absorption of nutrients in vivo.

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Probing the binding of two 19‐nortestosterone derivatives to human serum albumin: insights into the interactions of steroid hormone drugs with functional biomacromolecule

Cited by 10 publications

References 41 publications

Computational and spectroscopic analysis of interaction between food colorant citrus red 2 and human serum albumin

Computational and spectroscopic analysis of interaction between food colorant citrus red 2 and human serum albumin

Activation of catalase by pioglitazone: Multiple spectroscopic methods combined with molecular docking studies

Investigation and comparison of the binding between tolvaptan and pepsin and trypsin: Multi‐spectroscopic approaches and molecular docking

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