Binding assessment of two arachidonic-based synthetic derivatives of adrenalin with β-lactoglobulin: Molecular modeling and chemometrics approach

Gholami, Samira; Bordbar, Abdol‐Khalegh; Akvan, Nadia; Parastar, Hadi; Fani, Najmeh; Gretskaya, N. M.; Безуглов, В. В.; Haertlé, Thomas

doi:10.1016/j.bpc.2015.10.001

Cited by 3 publications

(3 citation statements)

References 36 publications

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“…The R g is a physical quantity that describes the tightness of the protein structure. The larger its value, the lower the protein density, also indicating that the protein has expanded . The data in Figure A–C showed that the average R g of complex systems was higher than for the free whey proteins, revealing that the protein tightness was reduced and the structure transformed into a loose state caused by FX binding.…”

Section: Resultsmentioning

confidence: 98%

“…The larger its value, the lower the protein density, also indicating that the protein has expanded. 43 The data in Figure 4A−C showed that the average R g of complex systems was higher than for the free whey proteins, revealing that the protein tightness was reduced and the structure transformed into a loose state caused by FX binding. To further realize the variation of the radius of gyration, the SASA values of free and FX-binding whey proteins were determined.…”

Section: Journal Of Agricultural and Food Chemistrymentioning

confidence: 96%

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Construction of Fucoxanthin Vector Based on Binding of Whey Protein Isolate and Its Subsequent Complex Coacervation with Lysozyme

Zhu

et al. 2019

J. Agric. Food Chem.

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In this study, a novel vector for fucoxanthin (FX) was constructed using the ligand-binding property of whey protein isolate and its subsequent heteroprotein complex coacervation with lysozyme. The results showed that FX could quench the intrinsic fluorescence of the whey protein isolate by a static mechanism, indicating that they could spontaneously form a nanocomplex through non-covalent interactions. Moreover, the structural and electrostatic properties of the resulting whey protein were different from those before the binding of FX, and this could be well explained by molecular dynamics simulation. The size and ζ-potential tests showed that when the whey protein isolate was combined with FX and then coacervated with lysozyme, the heteroprotein ratio and pH, which affect the coacervation process, also changed compared to those of the free whey protein isolate. FT-IR spectroscopy results showed that FX was successfully encapsulated into complex coacervates. In addition, the heteroprotein system exhibited a higher loading efficiency and also provided a better protection for FX in heating, storage, and simulated gastrointestinal environments.

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Section: Resultsmentioning

confidence: 98%

Section: Journal Of Agricultural and Food Chemistrymentioning

confidence: 96%

Construction of Fucoxanthin Vector Based on Binding of Whey Protein Isolate and Its Subsequent Complex Coacervation with Lysozyme

Zhu

et al. 2019

J. Agric. Food Chem.

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“…Also, it has been shown that epigallocatechin-3-gallate (EGCG) in thermally-induced BLG-EGCG conjugates are protected from oxidative degradation [23]. Because of good biocompatibility and biodegradability of milk proteins, BLG could be considered as natural carrier for lipidsoluble drugs [24,25] and hence would be a candidate for carrying of AA-5HT and related compounds in controlled drug delivery. Moreover, similar conformational changes and ligand binding mechanism between bovine BLG and beta lactoglobulin from other mammals such as goat, indicates that this protein from various sources may have analogous biological role and could be used as drug carrier [26].…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic and dynamic properties of arachidonoyl serotonin- β-lactoglobulin complex: A molecular modeling and chemometric study

Gholami

Bordbar

Akvan

2016

Journal of Photochemistry and Photobiology B: Biology

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UV-Vis absorption data of β-lactoglobulin (BLG) and arachidonoyl serotonin (AA-5HT) in BLG complex were examined and analyzed using chemometrics method. Analysis of the spectral data matrices by using the multivariate curve resolution-alternating least squares (MCR-ALS) algorithm resulted to the pure concentration calculation and spectral profiles resolution of the chemical constituents and the values of (6.433±0.019)×10(4)M(-1), (4.532±0.007)×10(4)M(-1), (3.364±0.010)×10(4)M(-1) and (2.977±0.013)×10(4)M(-1) as estimated equilibrium constants at 288, 293, 298 and 303K, respectively. The number of chemical constituents involved in the interaction which was extracted by PCA method were free and bound BLG. The spontaneity of the binding process and critical role of hydrogen bonding and van der Waals interactions in stabilizing protein-ligand complex have been designated by negative values of Gibbs free energy, entropy and enthalpy changes. Molecular docking study showed that AA-5HT binds to Val(41), Leu(39), Leu(54), Ile(71), Phe(82), Asn(90), Val(92), Phe(105), Met(107), Glu(108) with the free binding energy of -37.478kJ/mol. Computational studies predicted that in spite of serotonin (5HT) which anchors to the outer surface of BLG by hydrogen bonds, AA-5HT is situated in the calyx pose and stayed there during the entire time of simulation. This binding is accompanying with no apparent influence on secondary structure and partially destabilization of tertiary structure of BLG which pointed the suitability of this protein as drug carrier for AA-5HT.

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Beta–lactoglobulin–nutrition allergen and nanotransporter of different nature ligands therapy with therapeutic action

Varlamova

Zaripov

2020

Research in Veterinary Science

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Binding assessment of two arachidonic-based synthetic derivatives of adrenalin with β-lactoglobulin: Molecular modeling and chemometrics approach

Cited by 3 publications

References 36 publications

Construction of Fucoxanthin Vector Based on Binding of Whey Protein Isolate and Its Subsequent Complex Coacervation with Lysozyme

Construction of Fucoxanthin Vector Based on Binding of Whey Protein Isolate and Its Subsequent Complex Coacervation with Lysozyme

Spectroscopic and dynamic properties of arachidonoyl serotonin- β-lactoglobulin complex: A molecular modeling and chemometric study

Beta–lactoglobulin–nutrition allergen and nanotransporter of different nature ligands therapy with therapeutic action

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