The effect of glycation on bovine serum albumin conformation and ligand binding properties with regard to gliclazide

Żurawska-Płaksej, Ewa; Rorbach-Dolata, Anna; Wiglusz, Katarzyna; Piwowar, Agnieszka

doi:10.1016/j.saa.2017.08.071

Cited by 24 publications

(21 citation statements)

References 47 publications

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“…e maximum value of K q for a dynamic quenching process is 2 × 10 10 L•mol −1 •s −1 [25,30], and the values for the BSA-5d system were quite greater than the maximum value (Table 1). ese results suggest that static quenching was involved in BSA-5d interaction.…”

Section: Resultsmentioning

confidence: 93%

“…Site specific markers were used for identification of binding site studies using competitive binding experiments. e specific site markers phenylbutazone (PBT) for site I and ibuprofen (IBF) for site II of BSA were used to study the binding site involved in the competition with 5d (Figure 4) [24,25]. e spectra were recorded for BSA in presence of site marker holding the concentration of both constants and increasing 5d concentrations at room temperature (Figure 3(d)).…”

Section: Binding Constant Andmentioning

confidence: 99%

“…e uorescence quenching studies including synchronous and three-dimensional uorescence and UV spectroscopic studies were conducted to comprehend the binding mechanism between BSA and 5d. Binding site of 5d on BSA was established with ligand displacement studies using site probe ligands phenylbutazone for site I and ibuprofen for site II [24,25]. Molecular docking study for BSA and 5d interaction was also performed to corroborate with experimental results.…”

Section: Introductionmentioning

confidence: 97%

See 2 more Smart Citations

Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

Almehizia

Bakheit

Zargar

et al. 2019

Journal of Spectroscopy

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In this research, the pyrazoline pyridazine derivative 7-methyl-2-phenyl-4-(3,4,5-trimethoxyphenyl)-2H-pyrazolo[3,4-d]pyridazine (5d) was studied for its interaction with bovine serum albumin (BSA). Various spectroscopic techniques along with molecular docking analysis were utilized to understand the mechanism of interaction. The quenching of BSA fluorescence by using investigational drug 5d was the basic principle for the methodology. Spectrofluorometric methods and UV-absorption studies were conducted for exploration of the 5d and BSA binding mechanism. The fluorescence quenching mechanism involved in BSA and 5d interaction was static quenching, and a complex formation also occurred between them. Both enthalpy and entropy attained positive values suggesting involvement of hydrophobic forces in BSA and 5d interaction. The Förster distance of 2.23 nm was calculated by fluorescence resonance energy transfer (FRET). An alteration in BSA secondary structure was proven from the conformational studies of BSA-5d interaction. This binding interaction study provided a basis to comprehend the binding interaction between 5d and BSA. These results provided information about sites of BSA involved in its interaction with 5d.

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Section: Resultsmentioning

confidence: 93%

Section: Binding Constant Andmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

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Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

Almehizia

Bakheit

Zargar

et al. 2019

Journal of Spectroscopy

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“…The samples were collected every 7 days for up to 28 days. For the evaluation of the antiglycation compound by using the electrochemical chip, a fixed concentration of 40 g/L BSA or 2% gelatin was incubated with the hyperglycemic concentration of glucose (300 mg/dL) and inhibitory concentration of aspirin (40 mmol/L) [9,26,34,[37][38][39]. To inhibit the growth of any microorganism, 1 mmol sodium azide was supplemented in all the solutions.…”

Section: Glycation Of Proteins and Evaluation Of Antiglycation Compoundmentioning

confidence: 99%

“…Therefore, it is the most widely used protein to study the in vitro glycation. Bovine serum albumin (BSA) is a cost-efficient research strategy because it is inexpensive and possesses a high sequence and conformation homology with human serum albumin [26,27]. Moreover, BSA is considered as a model protein to investigate the effects of glycation, because of its abundance, and ease of purification [28][29][30].…”

Section: Introductionmentioning

confidence: 99%

An Electrochemical Chip to Monitor In Vitro Glycation of Proteins and Screening of Antiglycation Potential of Drugs

Khan

Park

2020

Pharmaceutics

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Hyperglycemia and the production of advanced glycation end products (AGEs) are the primary factors for the development of chronic complications in diabetes. The level of protein glycation is proportional to the glucose concentration and represents mean glycemia. In this study, we present an electrochemical chip-based method for in vitro glycation monitoring and the efficacy evaluation of an antiglycation compound. An electrochemical chip consisting of five microchambers and embedded microelectrodes was designed for parallel measurements of capacitance signals from multiple solutions at different concentrations. The feasibility of glycation monitoring was then investigated by measuring the capacitance signal at 0.13 MHz with bovine serum albumin and gelatin samples in the presence of various glucose concentrations over 28 days. A significant change in the capacitance due to protein glycation was observed through measurements conducted within 30 s and 21 days of incubation. Finally, we demonstrated that the chip-based capacitance measurement can be utilized for the selection of an antiglycation compound by supplementing the protein solution and hyperglycemic concentration of glucose with an inhibitory concentration of the standard antiglycation agent aspirin. The lack of a significant change in the capacitance over 28 days proved that aspirin is capable of inhibiting protein glycation. Thus, a strong relationship exists between glycation and capacitance, suggesting the application of an electrochemical chip for evaluating glycation and novel antiglycation agents.

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Biophysicochemical studies of a ruthenium (II) nitrosyl thioether‐thiolate complex binding to BSA: Mechanistic information, molecular docking, and relationship to antibacterial and cytotoxic activities

Shereef

Shaban

Moemen

et al. 2022

Applied Organom Chemis

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The purpose of this study was to extensively explore in vitro protein binding to [Ru (NO)(Et2NpyS4)]Br (RuNOTSP) and its ligand (TSP), correlate the findings with antibacterial and cytotoxic effects, and try to answer the question: Is the metal center always important for binding? With the aid of stopped‐flow and other spectroscopic and computational methods, the interaction between RuNOTSP and TSP and bovine serum albumin (BSA) was studied and a mechanism was proposed. From UV–Vis and fluorescence experiments, a static quenching mechanism and binding constants at a single site demonstrated the higher stability of the RuNOTSP‐BSA system at 298 K compared with TSP‐BSA. Stopped‐flow experiments indicated that binding of RuNOTSP and TSP to BSA is accomplished mainly via a two‐step mechanism: a fast second‐order binding followed by a slow first‐order isomerization process. The first reaction step is reversible with coordinate affinity Ka1 190 (RuNOTSP) and 50 M−1 (TSP). The second step for RuNOTSP is a reversible reaction with Ka2 of 76.4 M−1, whereas an irreversible step that was observed with a K2 of 0.18 M−1 for TSP indicates that TSP‐BSA is kinetically more stable than RuNOTSP‐BSA. The results revealed that the ruthenium center not only improves reaction rate through coordination affinity but also changes the binding process. Mode and strength of interaction of RuNOTSP and TSP with protein have also been supported by molecular docking and showed that RuNOTSP is located in IA pocket (Trp134) with a binding affinity (−7.27 kcal/mol), a slightly lower than TSP (−8.05 kcal/mol), and these results are in agreement with the binding constants. Furthermore, antibacterial testing revealed that RuNOTSP and TSP had high antibacterial activity against both Gram‐positive and Gram‐negative bacteria. They are also highly cytotoxic to HepG2 human liver cancer cells. Because the TSP‐BSA complex is kinetically more stable than that of RuNOTSP, the former illustrated better antibacterial and cytotoxic activities.

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The effect of glycation on bovine serum albumin conformation and ligand binding properties with regard to gliclazide

Cited by 24 publications

References 47 publications

Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

An Electrochemical Chip to Monitor In Vitro Glycation of Proteins and Screening of Antiglycation Potential of Drugs

Biophysicochemical studies of a ruthenium (II) nitrosyl thioether‐thiolate complex binding to BSA: Mechanistic information, molecular docking, and relationship to antibacterial and cytotoxic activities

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