An integrated approach with experimental and computational tools outlining the cooperative binding between 2-phenylchromone and human serum albumin

•The quenching mechanism of HSA by 2PHE is static.•2PHE has accessibility to Sites 1 and 2 of HSA.•The ligand binding has positive cooperative.•The interaction is entropically driven.•Molecular dynamic and docking match with experimental data. 2-Phenylchromone (2PHE) is a flavone, found in cereals a...

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Bibliographic Details
Published in:Food chemistry 2016-04, Vol.196, p.935-942
Main Authors: Caruso, Ícaro Putinhon, Filho, José Maria Barbosa, de Araújo, Alexandre Suman, de Souza, Fátima Pereira, Fossey, Marcelo Andrés, Cornélio, Marinônio Lopes
Format: Article
Language:English
Subjects:
2-Phenylchromone
Binding density function
Binding Sites
Chromones - chemistry
Computational methods
Computers, Molecular
Cooperative binding
Flavonoids - chemistry
Fluorescence spectroscopy
Human serum albumin
Humans
Molecular Dynamics Simulation
Protein Binding
Serum Albumin - chemistry
Spectrometry, Fluorescence - methods
Thermodynamics
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Summary:•The quenching mechanism of HSA by 2PHE is static.•2PHE has accessibility to Sites 1 and 2 of HSA.•The ligand binding has positive cooperative.•The interaction is entropically driven.•Molecular dynamic and docking match with experimental data. 2-Phenylchromone (2PHE) is a flavone, found in cereals and herbs, indispensable in the human diet. Its chemical structure is the basis of all flavonoids present in black and green tea, soybean, red fruits and so on. Although offering such nutritional value, it still requires a molecular approach to understand its interactions with a specific target. The combination of experimental and computational techniques makes it possible to describe the interaction between 2PHE and human serum albumin (HSA). Fluorescence spectroscopy results show that the quenching mechanism is static, and thermodynamic analysis points to an entropically driven complex. The binding density function method provides information about a positive cooperative interaction, while drug displacement experiments indicate Sites 1 and 2 of HSA as the most probable binding sites. From the molecular dynamic study, it appears that the molecular docking is in agreement with experimental data and thus more realistic.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2015.10.027