Investigation into the interaction of losartan with human serum albumin and glycated human serum albumin by spectroscopic and molecular dynamics simulation techniques: A comparison study

Moeinpour, Farid; Mohseni‐Shahri, Fatemeh S.; Malaekeh‐Nikouei, Bizhan; Nassirli, Hooriyeh

doi:10.1016/j.cbi.2016.07.025

Cited by 22 publications

(13 citation statements)

References 45 publications

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“…The distance r increased and the energy efficiency E decreased with increasing temperature, which resulted in the reduced stability of the binary systems and the values of K a . Moreover, the value of r was greater than R 0 in this study which suggested that RHB could strongly quench the intrinsic fluorescence of BSA by a static quenching mechanism [27]. In addition, from Table 5, the data obtained using the synchronous fluorescence spectrometry (∆λ = 60 nm) and fluorescence quenching method were basically consistent,…”

Section: Binding Distances Between Bsa-rhb Systemsupporting

confidence: 68%

Comparative Studies on the Interaction of Rhodamine B with Bovine Serum Albumin Using Fluorescence Method and Synchronous Fluorescence Method

Wang¹

2018

JCEBE

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The reaction mechanism of rhodamine B (RHB) with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy and synchronous fluorescence spectroscopy at different temperatures (298 K, 310 K and 318 K). The results showed that electrostatic force played a major role on the conjugation reaction between BSA and RHB, and the type of quenching was static quenching. Primary binding site for RHB was sub-hydrophobic domain IIA, and the number of binding sites was 1. The order of magnitude of binding constants (K a) was 10 4. The value of Hill's coefficients (n H) was approximately equal to 1, which suggested no cooperativity in BSA-RHB system. The donor-to-acceptor distance r < 7 nm indicated that the static fluorescence quenching of BSA by RHB was also a non-radiation energy transfer process. The results of two methods were consistent that showed the synchronous fluorescence spectroscopy could be used to study the reaction mechanism between drug and protein, and was a useful supplement to the conventional fluorescence quenching method.

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Section: Binding Distances Between Bsa-rhb Systemsupporting

confidence: 68%

Comparative Studies on the Interaction of Rhodamine B with Bovine Serum Albumin Using Fluorescence Method and Synchronous Fluorescence Method

Wang¹

2018

JCEBE

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“…k q is the bimolecular quenching constant and [L] is the concentration of the quencher, τ 0 is the average lifetime of fluorescence (about 10 -8 s) and K sv is the Stern-Volmer quenching constant. From Table 1, it could be seen that the k q value was greater than 2.0×10 10 L/mol•s at different temperatures 14 .The K sv value was inversely correlated with temperatures. The result indicated that the combination process of TTZ-PPL system was a static quenching process.…”

Section: Resultsmentioning

confidence: 87%

Exploring the Interaction of Tartrazine and Lipase: A Multispectroscopic Analysis, Docking and Computational Simulation Methods

Liu¹,

Zhang²,

Cheng³

2019

Asian J Pharm Res Dev

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The interaction between food colorant tartrazine and lipase was studied by multi-spectroscopic and molecular docking simulation under simulated physiological conditions to evaluate the toxic of tartrazine at the protein level. The results showed that tartrazine could effectively quench the endogenous fluorescence of lipase. The thermodynamic parameters were obtained from the van't Hoff equation, and the Gibbs free energy ΔG<0, indicating that the reaction was spontaneous; ΔH<0, ΔS>0, indicating hydrophobic interaction played a major role in forming the tartrazine-lipase complex. as shown by the synchronous fluorescence, UV-vis absorption and circular dichroism data, tartrazine could lead to the conformational and micro environmental changes of lipase, which may affect its physiological function. Molecular docking results showed that tartrazine was site in the active center of lipase, which altered the microenvironment of amino acid residues at the catalytic active center of lipase.

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“…The Scatchard equation is applied to evaluate the binding constant of ligand to protein ( Ka ) and the binding site number ( n ) is concerned with the binding interaction; it is given as [ 33 ] :

italiclog \frac{((), F_{0} - F)}{F} = italiclog K_{a} + italicnlog ([], Q)

…”

Section: Resultsmentioning

confidence: 99%

Bovine β‐casein binding studies of a Schiff base ligand: fluorescence and circular dichroism approaches

2020

Self Cite

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In this study, a Schiff base derived from a heterocyclic moiety was synthesized and characterized. The in vitro binding behaviour of this ligand with β‐casein (β‐CN) was investigated using biophysical techniques. For evaluation, thermodynamics variables of interactions between the Schiff base ligand and β‐CN, such as fluorescence at different temperatures, were measured. The results showed that the Schiff base ligand possessed considerable associated binding to β‐CN and that the procedure was enthalpy driven. The β‐CN conformation was also changed to give a further unfolded structure. Fluorescence resonance energy transfer was used to estimate the interval between donor (β‐CN) and acceptor (Schiff base ligand). All these experimental results proposed that β‐CN might act as carrier protein for the Schiff base ligand to deliver it to the target molecules.

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Investigation into the interaction of losartan with human serum albumin and glycated human serum albumin by spectroscopic and molecular dynamics simulation techniques: A comparison study

Cited by 22 publications

References 45 publications

Comparative Studies on the Interaction of Rhodamine B with Bovine Serum Albumin Using Fluorescence Method and Synchronous Fluorescence Method

Comparative Studies on the Interaction of Rhodamine B with Bovine Serum Albumin Using Fluorescence Method and Synchronous Fluorescence Method

Exploring the Interaction of Tartrazine and Lipase: A Multispectroscopic Analysis, Docking and Computational Simulation Methods

Bovine β‐casein binding studies of a Schiff base ligand: fluorescence and circular dichroism approaches

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