Effect of a Metal Ion in Modulating the Binding Interaction of a Dietary Flavonoid with Bovine Serum Albumin and DNA: A Spectroscopic and Theoretical Approach

Sengupta, P.; Pal, Uttam; Roy, Pritam; Samanta, Tapendu; Chattopadhyay, Nitin; Sen, Kamalika; Bose, Arup

doi:10.1021/acsfoodscitech.1c00361

Cited by 12 publications

(8 citation statements)

References 68 publications

(140 reference statements)

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“…The binding constants K a = 3.2× 10 5 , 7.1 × 10 5 , and 1.1 × 10 5 L·mol –1 and the number of binding sites n = 0.9, 2.2, and 1.2for Lut, Lut–Cu(II), and Cu(II) with BSA, respectively, were calculated by fitting according to the double-logarithm equation as shown in Figure g–i, and the results are summarized in Table . The results meant that Cu(II) coordination to Lut not only promoted one more Lut molecule further binding with BSA but also elevated the binding constants of Cu(II)–Lut, ∼2.2 times of Lut, which was different from Fe(II) coordination to rutin resulting in the decrease in binding constant and keeping mono-site binding with BSA as the parent rutin …”

Section: Resultsmentioning

confidence: 94%

“…The results meant that Cu(II) coordination to Lut not only promoted one more Lut molecule further binding with BSA but also elevated the binding constants of Cu(II)−Lut, ∼2.2 times of Lut, which was different from Fe(II) coordination to rutin resulting in the decrease in binding constant and keeping mono-site binding with BSA as the parent rutin. 52 3.1.3. Site-Specific Experiments.…”

Section: Resultsmentioning

confidence: 99%

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Double-Site Binding and Anti-/Pro-oxidation of Luteolin on Bovine Serum Albumin Mediated by Copper(II) Coordination

Song

Wang

et al. 2022

ACS Omega

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The interactions of luteolin (Lut) with bovine serum albumin (BSA) mediated by Cu(II) were investigated by spectroscopic, calorimetric, and molecular dynamic (MD) methods. Fluorescence studies showed that the binding of Lut to BSA was significantly enhanced by Cu(II) coordination with the number of binding sites and binding constant increasing from n = 1 and K a = 3.2 × 10 5 L·mol –1 for Lut to n = 2 and K a = 7.1 × 10 5 L·mol –1 for a 1:1 Cu(II)–luteolin complex, in agreement with the results from isothermal titration calorimetry (ITC). Site-specific experiments with warfarin and ibuprofen and MD confirmed that two binding sites of BSA were sequentially occupied by two Cu(II)–luteolin complexes. Cu(II) coordination increased the antioxidant activity of luteolin by 60% in the inhibition of carbonyl formation from the oxidation of amino groups in the side chain of BSA induced by the peroxyl radical ROO • ; however, it counteracted the antioxidant effects of luteolin and played pro-oxidative roles in BSA aggregation induced by • OH.

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Section: Resultsmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 99%

Double-Site Binding and Anti-/Pro-oxidation of Luteolin on Bovine Serum Albumin Mediated by Copper(II) Coordination

Song

Wang

et al. 2022

ACS Omega

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“…According to the report of Papadopoulou et al, quercetin showed a total quenching ability for the tryptophan fluorescence of BSA at a molar ratio of 10:1, whereas rutin required a molar ratio of approximately 25:1 . The presence of rutinose in rutin makes it less hydrophobic and bulkier than quercetin, increasing the steric hindrance of its penetration into the hydrophobic pocket of Trp-212 . As a result, the quenching effect of rutin on tryptophan residues was negatively affected.…”

Section: Resultsmentioning

confidence: 99%

“…34 The presence of rutinose in rutin makes it less hydrophobic and bulkier than quercetin, increasing the steric hindrance of its penetration into the hydrophobic pocket of Trp-212. 47 As a result, the quenching effect of rutin on tryptophan residues was negatively affected. The molecular docking results further support this observation.…”

Section: Effects Of Pef On the Composition Of Nf Samplesmentioning

confidence: 99%

Pulsed Electric Field Combined with Deep Eutectic Solvents Enhanced the Antiglycation Activity of Noni Flavonoid Extracts by Directionally Regulating Their Glycoside and Aglycone Proportions

Li,

Yu,

Liang

et al. 2024

ACS Sustainable Chem. Eng.

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This study aimed to develop a green and efficient approach based on pulsed electric field (PEF) in combination with deep eutectic solvents (DESs) to enhance the antiglycation ability of Noni flavonoids (NFs) by modulating their proportions of flavone glycosides and aglycones. The results showed that the proportion of quercetin was elevated with the increasing PEF treatment times at fixed treatment conditions (PEF conditions: 2 kV/cm, 30 μs, 10 Hz; DES: 100% choline chloride/oxalic acid). After 4000 PEF treatments, the molar ratio of rutin and quercetin in the NF sample changed from 0.92:0.08 to 0.09:0.91. Simultaneously, the inhibitory effects of the NF sample treated with 4000 pulses (NF4) on fructosamine, α-dicarbonyl, and advanced glycation end products (AGEs) in the bovine serum albumin (BSA)−fructose model were increased by 2.53, 2.98, and 1.23 times, respectively. This enhancement may be attributed to NF4 exhibiting a greater ability to bind protein and trap methylglyoxal (MGO) compared with untreated samples. Consequently, NF4 can more effectively prevent oxidative damage to the BSA structure, reducing protein aggregation and blocking the accumulation of AGEs. In summary, the combination of PEF with DESs presents a promising and sustainable method to effectively improve the antiglycation ability of Noni flavonoids, showing great potential for the functional food industry.

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“…The role of several drugs binding with BSA has been well explored in the literature through experimental and computational methods. − These methods have provided an immense source of information regarding the bimolecular interactions, binding affinity, and binding sites that are crucial for protein–ligand interactions . Herein, we have carried out the Mol.Doc method in analyzing the binding stability and the energetics of BSA site I and BSA site II drugs.…”

Section: Resultsmentioning

confidence: 99%

Complexity of the Role of Various Site-Specific and Selective Sudlow Binding Site Drugs in the Energetics and Stability of the Acridinedione Dye–Bovine Serum Albumin Complex: A Molecular Docking Approach

et al. 2023

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Molecular docking (Mol.Doc) techniques were employed to ascertain the binding affinity of two resorcinol-based acridinedione dyes (ADR1 and ADR2) with the widely studied globular protein Bovine Serum Albumin (BSA) in the presence of site-selective binding drugs by Autodock Vina 4.2 software. Docking of various feasible conformers of ADR1 dye with BSA was found to be energetically more favored than ADR2 dye, even though both these dyes differ in the 9th position of the basic dye structure. Analysis of dyes with BSA establishes the location of dye in all of the binding sites of BSA, predominantly through conventional and nonconventional hydrogen-bonding (HB) interactions. The coexistence of hydrophobic interactions resulted in the stability of various conformers generated. The introduction of site I and site II (Sudlow site binding drugs) into ADR1−BSA and ADR2−BSA complexes effectively destabilizes the dye−protein complex; however, the drugs do not displace ADR dyes completely from their selective binding domains. Site II binding drugs effectively destabilize the binding ability of the dye−protein complex rather than site I drugs. However, docking of site I drug 3-carboxyl-4-methyl-5-propyl-2-furanpropanic acid (CMPF) largely destabilizes the ADR1−protein complex, whereas indomethacin (INDO) enhances the binding affinity of the ADR2−protein complex. Interestingly, simultaneous docking of ADR dyes to the BSA−drug complex results in larger stability of the protein−drug complex through HB interactions rather than hydrophobic interactions. Both ADR1 and ADR2 dyes predominantly occupy the Sudlow binding sites of BSA, and the introduction of either site I or site II binding drugs does not displace the dye efficiently from the corresponding binding sites, rather the drugs are effectively displaced toward other binding domains apart from their specific site-binding domains of BSA. Through Mol.Doc techniques, we authenticate that the interactions in host−guest complex systems involving competing ligands are established in depth, wherein the dye as well as the amino acid (AA) moieties in BSA act as both HB donor and acceptor sites apart from several hydrophobic interactions coexisting toward the stability.

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Effect of a Metal Ion in Modulating the Binding Interaction of a Dietary Flavonoid with Bovine Serum Albumin and DNA: A Spectroscopic and Theoretical Approach

Cited by 12 publications

References 68 publications

Double-Site Binding and Anti-/Pro-oxidation of Luteolin on Bovine Serum Albumin Mediated by Copper(II) Coordination

Double-Site Binding and Anti-/Pro-oxidation of Luteolin on Bovine Serum Albumin Mediated by Copper(II) Coordination

Pulsed Electric Field Combined with Deep Eutectic Solvents Enhanced the Antiglycation Activity of Noni Flavonoid Extracts by Directionally Regulating Their Glycoside and Aglycone Proportions

Complexity of the Role of Various Site-Specific and Selective Sudlow Binding Site Drugs in the Energetics and Stability of the Acridinedione Dye–Bovine Serum Albumin Complex: A Molecular Docking Approach

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