Interaction Of Morin Research Articles

Bioactive potential of morin loaded mesoporous silica nanoparticles: A nobel and efficient antioxidant, antidiabetic and biocompatible abilities in in-silico, in-vitro, and in-vivo models

Developing a delivery system has become crucial in engineering cutting-edge next-generation theranostic approaches. Therefore, in the present research work, a customized Mesoporous silica nanoparticle (MSiNPs) was designed by adapting the Stöber method with silane polymerization for Morin (MO) adsorption. The average size of MSiNPs was 50–130 nm as measured by TEM, while FE-SEM revealed a spherical surface shape. According to Raman and FTIR spectra, while the synthesis of MSiNPs, CTAB (a surfactant) was eliminated from MSiNPs, silane was functionalized, and with a loading efficiency of 10.28 ± 0.22%, MO was adsorbed. Molecular docking was used to perform in-silico studies to investigate the interaction of native MO with antidiabetic and antioxidant enzymes. Furthermore, the antioxidant and antidiabetic effects of both MO adsorbed MSiNPs, and native MO were examined in vitro, with the former showing promise even at lower concentrations than the latter. The cell survival experiment on Mouse macrophages RAW 264.7 and HCT cells revealed that MO adsorbed MSiNPs were nontoxic up to 15 μg/ml. The acute toxicity of different concentrations of MO adsorbed MSiNPs was also conducted in an in vivo model zebrafish (Danio rerio), where the study was conducted for about 96 h and evaluated for histological significance. The findings described above revealed that the MSiNPs were electrochemically, structurally, and thermally stable and MO adsorbed MSiNPs were nontoxic and biocompatible, implying that it might be an effective drug delivery vehicle for MO in the future. Moreover, in coming times, this nano-delivery system with effective biodistribution of the adsorbed MO could be explored as an antidiabetic and anti-cancer agent.

Calorimetric, spectroscopic and computational investigation of morin binding effect on bovine serum albumin stability

The interaction of morin (Mor) with bovine serum albumin (BSA) was investigated using calorimetric, spectroscopic and computational methods. The ligand binding to protein has been studied under physiological conditions at various temperatures using isothermal titration calorimetry (ITC). Furthermore, the enthalpy (ΔH), entropy (ΔS) and heat capacity (ΔCp) changes of ligand-protein complex formation were also calculated. The results indicated two sites for Mor binding with BSA. The presence of Mor in higher concentration caused an increased thermal stability of protein proved by differential scanning calorimetry (DSC) measurements. Molecular docking and dynamics simulations supported Sudlow’s sites I and II of BSA as binding receptors for Mor. The dual action of ligand binding was demonstrated: stabilizer of the native protein structure up to the denaturation temperature and promoter of aggregation above this temperature.

The interaction of morin and morin-5’-sulfonic acid with lead(II): Study of the 1:1 complex formation process in aqueous solution

Abstract This article focuses on the aqueous complexation between two flavonoids (morin and morinsulfonate) and Pb2+ at constant ionic strength I=0.5 M (NaClO4). The determination of stability constants of ML complexes were performed at wide pH range. Two obtained constants are 14.8 ± 0.1 and 15.2 ± 0.1 logarithmic units for morin and morin-5’-sulfonic acid, respectively. For estimating the thermodynamic stability of the complexes studied, the Def2-SV(P)/DFT/PBE0/SMD method has been used. Different computational models were tested to describe the data obtained. The theoretical values of logK reproduce the experimental parameters within reasonable errors.

Computational and experimental validation of morin as adenosine deaminase inhibitor

Adenosine deaminase (ADA) is one of the major enzymes involved in purin metabolism, it has a significant role in cell growth and differentiation. Over-activity of ADA has been noticed in some pathology, like malignancy and inflammation and makes it an attractive target for the development of drugs for such diseases. In the present study, ADA inhibitory activity of morin, a bioactive flavonoid, was assessed through computational and biophysical methods. The enzyme kinetics data showed that morin is a competitive inhibitor of ADA. Binding energy calculated from ITC analysis was −7.11 kcal/mol. Interaction of morin with ADA was also studied using fluorescence quenching method. Molecular docking studies revealed the structural details of the interaction. Molecular dynamics study in explicit solvent was also conducted to assess the structural stability of protein ligand complex.

Spectroscopic and molecular modeling studies of the interaction between morin and polyamidoamine dendrimer

Interactions between the polyamidoamine (PAMAM) dendrimer and drug molecules are of interest for their potential biomedical applications. The goal of this work is to examine the interaction of PAMAM-C12 25% dendrimer with morin. The ultraviolet-visible, fluorescence spectroscopic methods as well as molecular modeling were used to analyze drug-binding mode, binding constants and binding sites, etc. The experimental data showed that the binding constant of morin-PAMAM-C12 25% is about 10(5) L/mol. The interaction of morin with PAMAM-C12 25% is mainly driven by the hydrophobic, electrostatic, hydrogen bonds and van der Waals forces. There are mainly three classes of binding site of morin at the interface of PAMAM-C12 25%. These results provided some useful information for self-assembling and disassembling the PAMAM dendrimer as well as efficient drug delivery and therapeutic applications.

Binding of antioxidant flavonol morin to the native state of bovine serum albumin: Effects of urea and metal ions on the binding

In consideration of the various medicinal aspects of the flavonoid polyphenols, the interaction of morin with bovine serum albumin (BSA) has been investigated using multi-spectroscopic approaches. The pKa1 of morin being 5.09, which is below physiological pH, binding studies provide important insights into its potential use as a biotherapeutic. The binding was performed under different pH (5, 7 and 9) conditions and in absence and presence of Cu(II) and Fe(III) ions. It is observed that the presence of metal ions affect the binding of morin towards BSA. The binding with BSA results in a motional restriction of morin in solution that causes an increase in anisotropy (r), rotational correlation time (tr) and steady-state lifetime (tav) of the ligand. Urea causes denaturation of BSA resulting in the release of morin from the protein core as determined from both the steady-state fluorescence and anisotropy (r) measurements. The possibility of non-radiative energy transfer from the donor tryptophan to the acceptor morin is detected following the Förster's theory. The site marker displacement studies along with the molecular docking results indicated that morin binds to the hydrophobic pocket of site 1 (subdomain IIA) near Trp 213 of BSA.

Structural analysis of DNA and RNA interactions with antioxidant flavonoids

Flavonoids are natural polyphynolic compounds with major antioxidant activity that can prevent DNA damage. The anticancer and antiviral activities of these natural products are attributed to their potential biomedical applications. In this review we are examining how the antioxidant flavonoids bind DNA and RNA and what mechanism of action is involved in preventing DNA damage. Detailed spectroscopic data on the interactions of morin (mor), apigenin (api), naringin (nar), quercetin (que), kaempferol (kae) and delphinidin (del) with DNA and transfer RNA in aqueous solution at physiological conditions were analysed. The structural analysis showed flavonoids mainly intercalate into DNA and RNA duplexes with minor external binding to the major or minor groove and the backbone phosphate group with overall binding constants for DNA adducts Kmor═5.99×103 M–1, Kapi═7.10×104 M–1, and Knar═3.10×103 M–1, Kque═7.25×104 M–1, Kkae═3.60×104 M–1 and Kdel═1.66×104 M–1, and for tRNA adducts Kmor═9.15×103 M–1, Kapi═4.96×104 M–1, and Knar═1.14×104 M–1, Kque═4.80×104 M–1, Kkae═4.65×104 M–1 and Kdel═9.47×104 M–1. The stability of adduct formation is in the order of que > api > kae > del >mor > nar for DNA and del > api > que > kae > nar > mor for tRNA. Low flavonoid concentration induces helical stabilization, whereas high pigment content causes helix opening. Flavonoids induce a partial B to A–DNA transition at high pigment concentration, while tRNA remains in A-family structure upon flavonoid complexation. The antioxidant activity of flavonoids changes in the order delphinidin > quercetin > kaempferol > morin > naringin > apigenin. The results show intercalated flavonoid molecule can act as an antioxidant and prevent DNA damage.

Structural analysis of DNA and RNA interactions with antioxidant flavonoids

Flavonoids are natural polyphynolic compounds with major antioxidant activity that can prevent DNA damage. The anticancer and antiviral activities of these natural products are attributed to their potential biomedical applications. In this review we are examining how the antioxidant flavonoids bind DNA and RNA and what mechanism of action is involved in preventing DNA damage. Detailed spectroscopic data on the interactions of morin (mor), apigenin (api), naringin (nar), quercetin (que), kaempferol (kae) and delphinidin (del) with DNA and transfer RNA in aqueous solution at physiological conditions were analysed. The structural analysis showed flavonoids mainly intercalate into DNA and RNA duplexes with minor external binding to the major or minor groove and the backbone phosphate group with overall binding constants for DNA adducts Kmor═5.99×103M–1, Kapi═7.10×104M–1, and Knar═3.10×103M–1, Kque═7.25×104M–1, Kkae═3.60×104M–1and Kdel═1.66×104M–1, and for tRNA adducts Kmor═9.15×103M–1, Kapi═4.96×104M–1, and Knar═1.14×104M–1, Kque═4.80×104M–1, Kkae═4.65×104M–1and Kdel═9.47×104M–1. The stability of adduct formation is in the order of que > api > kae > del >mor > nar for DNA and del > api > que > kae > nar > mor for tRNA. Low flavonoid concentration induces helical stabilization, whereas high pigment content causes helix opening. Flavonoids induce a partial B to A–DNA transition at high pigment concentration, while tRNA remains in A-family structure upon flavonoid complexation. The antioxidant activity of flavonoids changes in the order delphinidin > quercetin > kaempferol > morin > naringin > apigenin. The results show intercalated flavonoid molecule can act as an antioxidant and prevent DNA damage.

Probing the binding of morin to human serum albumin by optical spectroscopy

Morin [2-(2,4-dihydroxyphenyl)-3,5,7-trihydroxy-4H-1-benzopyran-4-one], a member of flavonols, is an important bioactive compound by interacting with nucleic acids, enzymes and protein. Its binding to human serum albumin was investigated by fluorescence quenching, fluorescence anisotropy, and UV–vis absorbance under the simulative physiological condition. Fluorescence quenching data show that the interaction of morin with HSA forms a non-fluorescent complex with the binding constants of 1.394 × 10 5, 1.489 × 10 5, 1.609 × 10 5 and 1.717 × 10 5 M −1 at 292, 298, 303 and 310 K, respectively. The thermodynamics parameters, enthalpy change (Δ H) and entropy change (Δ S) were calculated to be 8.97 kJ mol −1 and 129.15 J mol −1 K −1 via van’t Hoff equation. From the spectroscopic results and thermodynamics parameters, it is observed that van der Waals and hydrogen bonds are predominant intermolecular forces when forming the complex. The distance r = 4.25 nm between donor (Trp214) and accepter (morin) was estimated based on the Förster theory of non-radiative energy transfer. The red shift of UV–vis absorbance shows that morin is bound to several amino acids on the hydrophobic pocket of HSA. Moreover, the competitive probes, such as warfarin and ibuprofen (site I and II probes, respectively), reveal that the binding location of morin to HSA in the site I of the hydrophobic pocket, which corresponds to the results of UV–vis absorbance, while morin also binds other lower affinity binding sites on HSA from the fluorescence anisotropy spectroscopy.

Characterization of the interaction between human serum albumin and morin

The interaction of morin with human serum albumin (HSA) has been investigated by using fluorescence, UV absorption and Fourier transform infrared spectroscopic approaches for the first time. Fluorescence data revealed the presence of a specific binding site on HSA for morin, and the binding affinity was 1.13 ± 0.11 × 10 − 5 L Mol − 1 in the physiological condition. The intrinsic fluorescence of morin was conspicuously enhanced in the presence of HSA due to excited-state proton transfer. The binding ability of morin to protein decreased with the increase of the buffer pH from 6.4 to 8.4, which signified that the level of protonation of the hydroxyl groups played an important role during the drug–protein binding process. From the UV absorption spectra of morin in various pH medium, the dissociation behaviors of the hydroxyl groups on the drug molecule were assigned. The second derivative UV absorption spectra of morin after interacting with HSA were used to elucidate the binding mode of morin to protein. The obvious red shift of the UV absorption band I of morin upon binding to HSA further confirmed the formation of HSA–morin complex, and this property was also utilized to estimate the binding constant. The interaction between morin and HSA induced an obvious reduction of the protein α-helix and β-sheet structures.

Interaction of morin with CTMAB: aggregation and location in micellar

The aggregation and location of morin in CTMAB micellar solution was studied by light scattering spectra, electronic absorption spectra and pulsed FT NMR techniques. The difference in the light scattering property of morin with and without CTMAB proved that a large particle of the morin–CTMAB associate formed. Morin has a self-assembly tendency, but the assembly number is not high. With the increase of morin concentration, morin changed from a monomer to dimer. The hyperchromic and bathochromic effect of morin, with the increase in pH value or CTMAB concentration indicated that CTMAB provided a base microenvironment. The changes in the chemical shifts of the individual groups of protons in CTMAB indicated that the solubilization location of morin changes from the inner to the outer of the CTMAB micellar with an increase in morin concentration.

Interaction of morin-cetyltrimethylammonium bromide with nucleic acids and determination of nucleic acids at nanograms per milliliter levels based on the enhancement of preresonance light scattering.

A new preresonance light scattering (PRLS) assay of nucleic acids is presented. At pH 7.30, the weak PRLS of morin-cetyltrimethylammonium bromide (CTMAB) can be greatly enhanced by the addition of nucleic acids, owing to the interaction between the nucleic acid and morin-CTMAB. After the addition of morin and CTMAB to DNA, the zeta potential of DNA decreases and changes from negative to positive, which is due to the formation of an associate, the aggregation of morin on nucleic acids and the electric neutralization between DNA and the cationic surfactant CTMAB. Mechanism studies showed that the enhanced PRLS comes from the aggregation of morin in the presence of nucleic acids and CTMAB. The enhanced intensity of PRLS is in proportion to the concentration of nucleic acids in the range 7.5 x 10(-9)-1.0 x 10(-5) g ml(-1) for calf thymus DNA, 7.5 x 10(-9)-1.0 x 10(-6) g ml(-1) for salmon sperm DNA and 1.0 x 10(-8)-1.0 x 10(-6) g ml(-1) for yeast RNA. The detection limits are 3.4, 6.2 and 4.1 ng ml(-1) for calf thymus DNA, salmon sperm DNA and yeast RNA, respectively. Synthetic samples were analyzed satisfactorily.