Probing the interaction between 7-O-β-d-glucopyranosyl-6-(3-methylbut-2-enyl)-5,4′-dihydroxyflavonol with bovine serum albumin (BSA)

Chaves, Otávio Augusto; Cesarín-Sobrinho, Darí; Sant’Anna, Carlos Maurício R.; Carvalho, Mário Geraldo de; Suzart, Luciano Ramos; Catunda, Francisco Eduardo Aragão; Netto‐Ferreira, José Carlos; Ferreira, Aurélio B. B.

doi:10.1016/j.jphotochem.2016.12.015

Cited by 60 publications

(32 citation statements)

References 54 publications

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“…Since the fluorescence lifetime of HSA is unaffected by the presence of BZL, MTZ, NFX or MZ at a concentration of 1.15 × 10 -5 M, one can conclude that the fluorescence quenching mechanism is static, which implies a groundstate association between the tryptophan residue in HSA and the antiparasitic drugs. 11,14 These results are in total accordance with the results shown above for the steady state fluorescence quenching (ground-state association, Table 1). …”

Section: Time-resolved Fluorescence Studiessupporting

confidence: 91%

“…For BZL, MTZ and MZ, the entropy and enthalpy changes are responsible for the major contribution to the negative sign of ΔG°, indicating that the interaction between HSA with these samples is entropically and enthalpically driven. 14,28 On the other hand, for NFX only the entropy change is responsible for the major contribution to the negative sign of ΔG°, indicating that the interaction HSA:NFX is entropically driven. 31 Ross and Subramanian 33 have characterized the sign of the thermodynamic parameters with various kinds of interaction which may take place in the protein association process.…”

Section: Resultsmentioning

confidence: 99%

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Multiple Spectroscopic and Theoretical Approaches to Study the Interaction between HSA and the Antiparasitic Drugs: Benznidazole, Metronidazole, Nifurtimox and Megazol

Chaves¹,

Ferreira²,

Silva³

et al. 2018

J. Braz. Chem. Soc.

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The interaction between four antiparasitic drugs (benznidazole (BZL), metronidazole (MTZ), nifurtimox (NFX) and megazol (MZ)) with human serum albumin (HSA), the main vehicle of biodistribution of xenobiotics, hydrophobic, small and endogenous molecules in the bloodstream, was evaluated by multiple spectroscopic techniques and theoretical calculations. In all cases quenching of the fluorescence of HSA by these drugs involve a static mechanism, due to ground state association. There is just one main binding site in HSA for these four ligands (Sudlow's site I); binding is spontaneous, moderate, does not have any effect on the polarity around the Tyr and Trp residues and does not perturb significantly the secondary structure of the protein. Molecular docking studies suggest hydrogen bonding and hydrophobic interactions as the main binding forces, i.e., BZL associates with the Trp-214 residue via hydrophobic interactions and with Gln-220, Arg-221 and Glu-449 residues via hydrogen bonding; whereas MTZ associates with Leu-197 and Leu-480 residues via hydrophobic interactions and with Trp-214, Glu-449 and Ser-453 via hydrogen bonding. Furthermore, electrostatic interactions were also suggested for HSA:MZ and HSA:NFX.

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Section: Time-resolved Fluorescence Studiessupporting

confidence: 91%

Section: Resultsmentioning

confidence: 99%

Multiple Spectroscopic and Theoretical Approaches to Study the Interaction between HSA and the Antiparasitic Drugs: Benznidazole, Metronidazole, Nifurtimox and Megazol

Chaves¹,

Ferreira²,

Silva³

et al. 2018

J. Braz. Chem. Soc.

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“…, indicating that the 1,4-naphthoquinone derivatives under study can interact moderately with serum albumin. 44,45 In addition, the decrease in the K b values with the increase of temperature suggests the lesser stability of HSA:1,4-naphthoquinone derivatives complex at higher temperature, being in full accordance with the existence of a static fluorescence quenching mechanism as described above.…”

Section: Spectroscopic Analysis Of the Interaction Hsa:fnp And Hsa:fnmentioning

confidence: 67%

Drug-Protein Interaction: Spectroscopic and Theoretical Analysis on the Association between HSA and 1,4- Naphthoquinone Derivatives

Ferreira¹,

Chaves²,

Oliveira³

et al. 2018

Rev. Virtual Quim.

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Resumo: A interação entre albumina sérica humana (ASH) e dois derivados biologicamente ativos de 1,4-naftoquinona (FNP e FNP4Br) foi estudada por dicroísmo circular, fluorescência estacionária e fluorescência resolvida no tempo sob condições biológicas a 305 K, 310 K e 315 K. Para oferecer uma explicação a nível molecular, foram realizados cálculos de ancoramento molecular. Uma associação no estado estacionário entre a albumina e as amostras foi observada por estudos espectroscópicos. A ligação é espontânea, moderada, pode perturbar a estrutura secundária da albumina e aumentar a hidrofobicidade ao redor do resíduo Trp-214, isso provavelmente devido a efeitos hidrofóbicos. Parâmetros termodinâmicos e ancoramento molecular sugerem ligação de hidrogênio e interações eletrostáticas (dipolo-dipolo) como as principais forças para a associação ASH:FNP e ASH:FNP4Br.Palavras-chave: Albumina sérica humana; Derivados de 1,4-naftoquinona; Espectroscopia; Ancoramento molecular. AbstractThe interaction between human serum albumin (HSA) and two biologically active 1,4-naphthoquinone derivatives (FNP and FNP4Br) was studied by circular dichroism, steady-state and time-resolved fluorescence under biological conditions at 305 K, 310 K and 315 K. In order to offer a molecular level explanation, molecular docking calculations were carried out. A ground state association between albumin and the samples was observed by spectroscopic studies. The binding is spontaneous, moderate, can perturb the secondary structure of the albumin and increase the hydrophobicity around the Trp-214 residue, probably due the hydrophobic effect. Thermodynamic parameters and molecular docking results suggest hydrogen bonding and electrostatic interactions (dipole-dipole) as the main binding forces for the association HSA:FNP and HSA:FNP4Br.

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“…Since n values were approximately 1.00 for all temperatures (Table 1), this is a clear indication that a single binding site is available for MHDCTN and PHDCTN on the HSA structure. 20 Knowing the n value, the binding constant (K a ) for the association between HSA and the two semi-synthetic compounds can be calculated employing a modified Stern-Volmer analysis (equation 3) 31 ( Figure S4, SI section). For both quenchers, the K a value is in the order of 10 5 M -1…”

Section: Hsa Binding Studiesmentioning

confidence: 99%

“…This provides a clear indication that the microenvironment around the aromatic amino acids residues Trp and Tyr does not change with the presence of the potential anti-cancer agents under study. 31 Perturbation on the secondary structure of the protein In order to identify possible structural changes in the HSA structure upon MHDCTN or PHDCTN binding, circular dichroism (CD) experiments were carried out. The CD spectrum of HSA at physiological pH exhibits two negative bands in the ultraviolet region at 208 nm (π → π* transition) and at 222 nm (n → π* transition), which are characteristics of the α-helical content.…”

Section: Synchronous Fluorescence Analysismentioning

confidence: 99%

In vitro Analysis of the Interaction between Human Serum Albumin and Semi‑Synthetic Clerodanes

Chaves¹,

Echevarrı́a²,

Esteves-Souza³

et al. 2018

J. Braz. Chem. Soc.

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The interaction between HSA and two semi-synthetic potential anti-cancer agents derived from trans-dehydrocrotonin-methyl-hydrazone (MHDCTN) and phenyl-hydrazone (PHDCTN) was evaluated under physiological conditions at 296, 303 and 310 K by multi-spectroscopic techniques and molecular docking calculations. Steady state fluorescence quenching indicated a ground state association (static quenching) for both samples; however, the quenching induced by PHDCTN was not essentially static and can be accompanied by a dynamic quenching mechanism. The binding is strong (modified Stern-Volmer binding constant (K a ) ca. 10 5 M -1 ), causing a very weak perturbation on the secondary structure of the protein and there is just one main binding site for both samples (Sudlow's site I). Molecular docking results suggested hydrogen bonding and hydrophobic interactions as the main binding forces for both samples.

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Probing the interaction between 7-O-β-d-glucopyranosyl-6-(3-methylbut-2-enyl)-5,4′-dihydroxyflavonol with bovine serum albumin (BSA)

Cited by 60 publications

References 54 publications

Multiple Spectroscopic and Theoretical Approaches to Study the Interaction between HSA and the Antiparasitic Drugs: Benznidazole, Metronidazole, Nifurtimox and Megazol

Multiple Spectroscopic and Theoretical Approaches to Study the Interaction between HSA and the Antiparasitic Drugs: Benznidazole, Metronidazole, Nifurtimox and Megazol

Drug-Protein Interaction: Spectroscopic and Theoretical Analysis on the Association between HSA and 1,4- Naphthoquinone Derivatives

In vitro Analysis of the Interaction between Human Serum Albumin and Semi‑Synthetic Clerodanes

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