scholarly journals Interactions between β-Lactoglobulin and 3,3′-Diindolylmethane in Model System

Molecules ◽  
2019 ◽  
Vol 24 (11) ◽  
pp. 2151 ◽  
Author(s):  
Cuina Wang ◽  
Xinhui Zhou ◽  
Hao Wang ◽  
Xiaomeng Sun ◽  
Mingruo Guo
Keyword(s):  
Tight Binding ◽  
Model System ◽  
Anticancer Activities ◽  
Enhanced Fluorescence ◽  
Uv Absorption Spectra ◽  
Potential Value ◽  
Ft Ir ◽  
Β Lactoglobulin ◽  
Β Sheet ◽  
Good Vehicle

The compound 3,3′-diindolylmethane (DIM) has a broad spectrum of anticancer activities. However, low stability and bioavailability limit its application. Elucidating interactions between DIM and β-lactoglobulin (β-LG) may be useful for fabricating whey protein-based protecting systems. Interaction with DIM increased the diameter and absolute zeta potential value of β-LG. UV-absorption spectra suggested that there was a complex of DIM and β-LG. β-LG showed enhanced fluorescence intensity by complexing with DIM with a binding constant of 6.7 × 105 M−1. Upon interaction with DIM, β-LG was decreased in secondary structure content of helix and turn while increased in β-sheet and unordered. FT-IR spectra and molecular docking results indicated the roles of hydrophobic interaction and hydrogen bond for the formation of DIM and β-LG nanocomplexes. Data suggested that β-LG may be a good vehicle for making a protein-based DIM protection and delivery system due to the tight binding of DIM to β-LG.

A Study of the Amide III Band by FT-IR Spectrometry of the Secondary Structure of Albumin, Myoglobin, and γ-Globulin

1987 ◽  
Vol 41 (2) ◽  
pp. 180-184 ◽  
Author(s):  
Koichi Kaiden ◽  
Tomoko Matsui ◽  
Shigeyuki Tanaka
Keyword(s):  
Secondary Structure ◽  
Conformational Changes ◽  
Phosphate Buffer Solution ◽  
Heat Denaturation ◽  
Buffer Solution ◽  
Ir Spectrometry ◽  
Ft Ir ◽  
Α Helix ◽  
Β Lactoglobulin ◽  
Β Sheet

FT-IR spectrometry was applied to the identification of the secondary structure species of a living protein. The spectra of native myoglobin and albumin were obtained with methods using either KBr pellet or film formed on a KBr window from an aqueous solution. Pellet preparation of myoglobin and albumin caused the structure to change from α-helix to β-structure. The conformational changes that arise from heat denaturation of myoglobin, albumin, and γ-globulin were observed by the changes in the amide I, II, and III bands. The bands of the 1300, 1260, and 1235 cm−1 regions were respectively assigned to α-helix, disordered, and β-sheet structures. These band positions were substantiated by the spectra of β-lactoglobulin and α-casein. α-Helix structure probably changes to β-structure in the presence of alkali halide, and changes to disordered structure with heat denaturation in phosphate buffer solution. The secondary structure of a protein is further identified by use of the information obtained from the amide I, II, and III bands; the amide III band is especially important. Furthermore, it may be possible to characterize the species of secondary structures of proteins adsorbed on material surfaces.

Synthesis of New α-Amino Phosphonates Containing 3-Amino-4(3H) Quinazolinone Moiety as Anticancer and Antimicrobial Agents: DFT, NBO, and Vibrational Studies

2018 ◽  
Vol 15 (2) ◽  
pp. 286-296 ◽  
Author(s):  
Mohamed K. Awad ◽  
Mahmoud F. Abdel-Aal ◽  
Faten M. Atlam ◽  
Hend A. Hekal
Keyword(s):  
Biological Activity ◽  
Cell Line ◽  
Quantum Chemical ◽  
Density Functional ◽  
Carcinoma Cell ◽  
Liver Carcinoma ◽  
Anticancer Activities ◽  
Functional Theory ◽  
Ft Ir ◽  
Good Agreement

Aim and Objective: Synthesis of new .-aminophosphonates containing quinazoline moiety through Kabachnik-Fields reaction in the presence of copper triflate catalyst [32], followed by studying their antimicrobial activities and in vitro anticancer activities against liver carcinoma cell line (HepG2) with the hope that new anticancer agents could be developed. Also, the quantum chemical calculations are performed using density functional theory (DFT) to study the effect of the changes of molecular and electronic structures on the biological activity of the investigated compounds. Materials and Method: The structures of the synthesized compounds are confirmed by FT-IR, 1H NMR, 13C NMR, 31P NMR and MS spectral data. The synthesized compounds show significant antimicrobial and also remarkable cytotoxicity anticancer activities against liver carcinoma cell line (HepG2). Density functional theory (DFT) was performed to study the effect of the molecular and electronic structure changes on the biological activity. Results: It was found that the electronic structure of the substituents affects on the reaction yield. The electron withdrawing substituent, NO2 group 3b, on the aromatic aldehydes gave a good yield more than the electron donating substituent, OH group 3c. The electron deficient on the carbon atom of the aldehydic group may increase the interaction of the Lewis acid (Cu(OTf)2) and the Lewis base (imine nitrogen), and accordingly, facilitate the formation of imine easily, which is attacked by the nucleophilic phosphite species to give the α- aminophosphonates. Conclusion: The newly synthesized compounds exhibit a remarkable inhibition of the growth of Grampositive, Gram-negative bacteria and fungi at low concentrations. The cytotoxicity of the synthesized compounds showed a significant cytotoxicity against the liver cancer cell line (HepG 2). Also, it was shown from the quantum chemical calculations that the electron-withdrawing substituent increases the biological activity of the α-aminophosphonates more than the electron donating group which was in a good agreement with the experimental results. Also, a good agreement between the experimental FT-IR and the calculated one was found.

Is folding of β-lactoglobulin non-hierarchic? intermediate with native-like β-sheet and non-native α-helix 1 1Edited by C. R. Matthews

2000 ◽  
Vol 296 (4) ◽  
pp. 1039-1051 ◽  
Author(s):  
Vincent Forge ◽  
Masaru Hoshino ◽  
Kazuo Kuwata ◽  
Munehito Arai ◽  
Kunihiro Kuwajima ◽  
...  
Keyword(s):  
Α Helix ◽  
Β Lactoglobulin ◽  
Β Sheet

scholarly journals New derivatives of a natural nordentatin

2020 ◽  
Vol 18 (1) ◽  
pp. 890-897 ◽  
Author(s):  
Tin Myo Thant ◽  
Nanik Siti Aminah ◽  
Alfinda Novi Kristanti ◽  
Rico Ramadhan ◽  
Hnin Thanda Aung ◽  
...  
Keyword(s):  
Cell Line ◽  
Parent Compound ◽  
T47d Cell ◽  
Positive Control ◽  
Inhibition Assay ◽  
Anticancer Activities ◽  
Methanol Fraction ◽  
T47d Cell Line ◽  
Ft Ir ◽  
Derivatives Of

AbstractNew derivatives were obtained from natural nordentatin (1) previously isolated from the methanol fraction of Clausena excavata by an acylation method. Herein, we report ten new pyranocoumarin derivatives 1a–1j. Their structures were elucidated based on UV-vis, FT-IR, NMR, and DART-MS data. The α-glucosidase inhibition and anticancer activities of nordentatin (1) and its derivatives were also evaluated. The α-glucosidase inhibition assay exhibited that the derivatives 1b, 1d, 1e, 1f, 1h, 1i, and 1j possess higher inhibitory activity for α-glucosidase with IC50 values of 1.54, 9.05, 4.87, 20.25, 12.34, 5.67, and 2.43 mM, whereas acarbose was used as the positive control, IC50 = 7.57 mM. All derivatives exhibited a weak cytotoxicity against a cervical cancer (HeLa) cell line with the IC50 between 0.25 and 1.25 mM. They also showed moderate to low growth inhibition of a breast cancer (T47D) cell line with IC50 values between 0.043 and 1.5 mM, but their activity was lower than that of the parent compound, nordentatin (1) (IC50 = 0.041 mM).

Time evolution of β-lactoglobulin corona formation on gold nanoparticles and impact on allergy

2020 ◽  
Author(s):  
Xiaoning Zhang ◽  
Meifeng Li ◽  
Yuanping Lv ◽  
Xiaoling Sun ◽  
Yao Han ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Secondary Structure ◽  
Time Evolution ◽  
Electrostatic Force ◽  
Protein Corona ◽  
Raw Milk ◽  
Covalent Bonds ◽  
Corona Formation ◽  
Β Lactoglobulin ◽  
Β Sheet

Abstract Gold nanoparticles (AuNPs) are modified immediately by the adsorption of β-lactoglobulin (βlg) when designed as colorimetric probe in raw milk, leading to the formation of a protein corona. This adsorption results mainly from a fast electrostatic force and a slow formation of Au-S covalent bonds, which is a precondition for the use of AuNPs in biodetection. The proteins corona influences the structure and bioactivity of adsorbed protein, such as the allergy. In this study, the mechanism of βlg adsorbed on AuNPs was investigated in terms of stoichiometry, binding affinity (Ka), time evolution of Au-S bond, and general secondary structure changes to address the desensitization of AuNPs. The results show that about 3,600 βlg are adsorbed on a single AuNPs, and the Ka is 2.9 ± 0.7 × 10 6 M -1 . The formation of Au-S bonds takes about 9 h, which is the time needed for complete changes in secondary structure and the IgE combining capacity. The structure of allergenic epitopes assigned to β-sheet was destroyed by the formation of Au-S bond, then induced to the decrease allergy. Furthermore, Fourier transform infrared spectroscopy confirmed a decrease in β-sheet contents after conjugated with AuNPs.

scholarly journals Synthesis and Characterization of 2-Pyrazoline Derivatives and their in silico and in vitro Studies on Antimicrobial and Anticancer Activities

2019 ◽  
Vol 31 (10) ◽  
pp. 2191-2196 ◽  
Author(s):  
S. Rathinamanivannan ◽  
K. Megha ◽  
Raja Chinnamanayakar ◽  
Ashok Kumar ◽  
M.R. Ezhilarasi
Keyword(s):  
Breast Cancer ◽  
Synthesis And Characterization ◽  
Anticancer Activities ◽  
1H And 13C Nmr ◽  
Chemical Structures ◽  
Ft Ir ◽  
Affinity Score ◽  
High Binding Affinity

The new series of 1-(4,5-dihydro-5-phenyl-3-diphenylpyrazol-1-yl)butan-1-one derivatives were synthesized by cyclization method using biphenyl chalcone with n-butyric acid and hydrazine hydrate. The synthesized 1-(4,5-dihydro-5-phenyl-3-diphenylpyrazol-1-yl)butan-1-one derivatives chemical structures were confirmed from spectral data such as FT-IR, 1H and 13C NMR. 2-Pyrazoline derivatives were docked with bacterial (1UAG) and breast cancer (1OQA) protein. Based on high binding affinity score, the best compound was subjected to in vitro anticancer activity by MTT assay. Also, antimicrobial activity were studied for synthesized 2-pyrazoline derivatives.

The Hydrogen-Bonded 2-Pyridone Dimer Model System. 1. Combined NMR and FT-IR Spectroscopy Study

2010 ◽  
Vol 114 (29) ◽  
pp. 7749-7760 ◽  
Author(s):  
Łukasz Szyc ◽  
Jing Guo ◽  
Ming Yang ◽  
Jens Dreyer ◽  
Peter M. Tolstoy ◽  
...  
Keyword(s):  
Ir Spectroscopy ◽  
Model System ◽  
Spectroscopy Study ◽  
Dimer Model ◽  
Ft Ir ◽  
System 1 ◽  
Ft Ir Spectroscopy ◽  
Hydrogen Bonded

Structural Characterization of β-Lactoglobulin in Solution Using Two-Dimensional FT Mid-Infrared and FT Near-Infrared Correlation Spectroscopy

1997 ◽  
Vol 51 (4) ◽  
pp. 536-540 ◽  
Author(s):  
Nelson L. Sefara ◽  
Noel P. Magtoto ◽  
Hugh H. Richardson
Keyword(s):  
Near Infrared ◽  
Spectral Response ◽  
Correlation Spectroscopy ◽  
Two Dimensional ◽  
Helical Structures ◽  
Β Sheets ◽  
Α Helix ◽  
Combination Bands ◽  
Β Lactoglobulin ◽  
Β Sheet

Two-dimensional (2D) FT-IR correlation analysis was applied to both the mid-IR (MIR) and near-IR (NIR) regions to investigate changes in the secondary structures of β-lactoglobulin in D2O (or H2O) solvent systems consisting of varying concentrations of bromoethanol. Mid-IR correlation spectra indicate that the amide I bands corresponding to different structures (i.e., α-helical structures at 1650 cm−1, aggregated β-strands at 1620 cm−1, and β-sheet at 1636 cm−1) exhibit apparently different spectral response towards varying concentrations of bromoethanol. We propose that the mechanism for the conversion of the β-sheet into α-helix occurs in terms of two parallel pathways, i.e., (1) β-sheets → aggregated β-strands →α-helix, and (2) β-sheets →α-helix. Although the amide B/amide II combination bands give no spectral features relating to the secondary structure, changes were found in the C–H combination bands that suggest an interaction between the solvent and the protein.

Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system

2003 ◽  
Vol 70 (1) ◽  
pp. 61-71 ◽  
Author(s):  
Younghee Cho ◽  
Harjinder Singh ◽  
Lawrence K Creamer
Keyword(s):  
Heat Stability ◽  
Model System ◽  
Hydrophobic Association ◽  
Milk Product ◽  
Disulphide Bonds ◽  
Sds Page ◽  
Β Lactoglobulin ◽  
Circular Dichroïsm ◽  
Product Functionality ◽  
Bonding Patterns

The interaction of κ-casein and β-lactoglobulin is fundamental to all heat-induced modifications of milk product functionality, such as the heat stability of concentrated milks. Purified native κ-casein B and β-lg A solutions were heated at 80 °C at pH 6·7 separately and in a mixture. The circular dichroism spectra in the near UV indicated irreversible changes in the disulphide bonding patterns involving both proteins. Alkaline- and SDS-PAGE of heated samples showed that, in the presence of κ-casein, less β-lg was converted into β-lg polymers and the rate of loss of native β-lg was greater. When κ-casein was added to previously heated β-lg and the mixture was heated, the κ-casein reacted with the heat-induced β-lg polymers more readily than with the β-lg native monomers. The formation of β-lg dimers, trimers etc. was diminished. It was concluded that, when β-lg and κ-casein were heated together, β-lg formed thiol-exposed monomers, which reacted with each other or with the native κ-casein depending on the relative concentrations of β-lg and κ-casein. The products of these reactions included some disulphide-bonded 1[ratio ]1 β-lg[ratio ]κ-casein complexes, some monomer κ-casein and a range of large aggregates held together by either or both disulphide bonds and hydrophobic association.

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