Binding of biogenic and synthetic polyamines to β-lactoglobulin

Essemine, J.; Hasni, Imed; Carpentier, Robert; Thomas, Thresia; Tajmir-Riahi, H.A.

doi:10.1016/j.ijbiomac.2011.04.016

Cited by 82 publications

(31 citation statements)

References 40 publications

(71 reference statements)

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“…The increases in β-sheet and α-helix contents and decreases in random coil content are indicative of structural stabilization in the presence of a ligand. Increases in random coil content as well as decreases in β-sheet and α-helix contents in the presence of a ligand pinpoint the fact that the protein structure is unstable [9]. The results of CD spectroscopy are shown in Fig.…”

Section: Resultsmentioning

confidence: 96%

“…All other reagents were of analytical grade. The β-LG concentrations in solution were determined spectrophotometrically at 278 nm using, for calculation, a molar absorption coefficient of ε=17,600 M −1 cm −1 [9].…”

Section: Methodsmentioning

confidence: 99%

“…One of them-Trp 19-is located on the A strand and is buried in the hydrophobic cavity, while the second-Trp 61-is accessible to solvent and is placed on external loop CD [10,39]. Previous work reported that the fluorescence contribution from β-LG Trp 19 is superior to the contribution of Trp 61, which is placed in an apolar environment [9] and is near the disulfide bond (Cys61-Cys166) acting as a powerful fluorescence quencher. Another cause of the low fluorescence yield of Trp 61 is its accessibility to polar solvent [14].…”

Section: Fluorescence Spectroscopymentioning

confidence: 99%

“…β-Strands A-H form a calyx (or β-barrel). A unique α-helix is located at the outer surface of the β-barrel, sticking to the β-strand H beyond the calyx [9,48]. The BC, DE, and FG as well as AB, CD, EF, and GH loops at the close and open ends of the calyx connect the β-strands, respectively [39].…”

Section: Introductionmentioning

confidence: 99%

“…The BC, DE, and FG as well as AB, CD, EF, and GH loops at the close and open ends of the calyx connect the β-strands, respectively [39]. Essemine et al have reported that β-LG interacts with various hydrophobic and amphiphilic ligands [9]. Previous work reported that β-LG has several sites for ligand binding [48].…”

Section: Introductionmentioning

confidence: 99%

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Probing of the Interaction Between β-Lactoglobulin and the Anticancer Drug Oxaliplatin

Ghalandari¹,

Divsalar²,

Eslami-Moghadam³

et al. 2014

Appl Biochem Biotechnol

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The potential carrier role of β-lactoglobulin (β-LG) and its interactions with oxaliplatin were studied using various spectroscopic techniques (fluorescence, UV-visible, and circular dichroism (CD)) in an aqueous medium at two temperatures of 25 and 37 °C in combination with a molecular docking study. Fluorescence measurements have shown that the observed quenching is a combination of static and dynamic quenching with a predominant contribution of static mode. The presence of a single binding site located in the internal cavity of the β-barrel of β-LG was confirmed by molecular docking calculations. Thermodynamic data as well as molecular docking indicated that the hydrophobic interactions dominate in the binding site. Results of fluorescence resonance energy transfer (FRET) measurements in combination with docking results imply that resonance energy transfer occurs between β-LG and its ligand oxaliplatin. Additionally, CD results revealed that oxaliplatin binding has no influence on the β-LG structure. The molecular docking results indicate that docking may be an appropriate method for the prediction and confirmation of experimental results. Complementary molecular docking results may be useful for the determination of the binding mechanism of proteins such as β-LG in pharmaceutical and biophysical studies providing new insight in the novel pharmacology and new solutions in the formulation of advanced oral drug delivery systems.

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Section: Resultsmentioning

confidence: 96%

Section: Methodsmentioning

confidence: 99%

Section: Fluorescence Spectroscopymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Probing of the Interaction Between β-Lactoglobulin and the Anticancer Drug Oxaliplatin

Ghalandari¹,

Divsalar²,

Eslami-Moghadam³

et al. 2014

Appl Biochem Biotechnol

View full text Add to dashboard Cite

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Protein‐based nanoparticles as matrices for encapsulation of lipophilic nutraceuticals

Pérez¹,

Sponton²,

Santiago³

2016

New Polymers for Encapsulation of Nutraceutical Compounds

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A multidisciplinary study for investigating the interaction of an iron complex with bovine liver catalase

Hashemizadeh

Shiri

Shahraki

et al. 2022

Applied Organom Chemis

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Catalase (CAT) is an essential protein protecting the cell from oxidative damage by reactive oxygen species. CAT is a heme enzyme in which iron metal plays a crucial role in catalytic activity. In this research, an iron (II, III) complex ([Fe (bpy) 3 ] [Fe (dipic) 2 ] 2 .7H 2 O; dipic À2 = pyridine-2,6-dicarboxylato and bpy = 2,2 0 -bipyridine) was used to evaluate its binding interactions with bovine liver catalase (BLC) using spectroscopic and molecular docking methods. The experimental results demonstrated that the catalytic activity of BLC increased slightly and reached 106% of the initial activity. The interactions between Fe complex and BLC led to the quenching of the catalase fluorescence emission via the static quenching mechanism. Thermodynamic parameters demonstrated that the predominant interactions between catalase and Fe complex are hydrogen bond and van der Waals and the process is exothermic and enthalpy driven. The circular dichroism (CD) and synchronous fluorescence results showed that the Fe complex altered the structure and conformation of BLC. It changed the secondary structure of BLC by decreasing α-helix and β-sheet content. Also, the experimental data were analyzed using Multivariate Curve Resolution-Alternating Least Square (MCR-ALS) to the resolution of measured complex spectra and estimate the number of independent chemical species. The docking results in agreement with experimental data showed that the cationic part of the complex with catalase is mainly hydrophobic and van der Waals interactions, and for the anionic part are hydrophobic, van der Waals, and hydrogen bonding.

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Binding of biogenic and synthetic polyamines to β-lactoglobulin

Cited by 82 publications

References 40 publications

Probing of the Interaction Between β-Lactoglobulin and the Anticancer Drug Oxaliplatin

Probing of the Interaction Between β-Lactoglobulin and the Anticancer Drug Oxaliplatin

Protein‐based nanoparticles as matrices for encapsulation of lipophilic nutraceuticals

A multidisciplinary study for investigating the interaction of an iron complex with bovine liver catalase

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