• Title/Summary/Keyword: P-M interaction

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Interaction of Resveratrol and Genistein with Nucleic Acids

  • Usha, Subbiah;Johnson, Irudayam Maria;Malathi, Raghunathan
    • BMB Reports
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    • v.38 no.2
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    • pp.198-205
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    • 2005
  • Resveratrol (RES) and genistein (GEN) are the dietary natural products known to possess chemopreventive property and also the ability to repair DNA damage induced by mutagens/carcinogens. It is believed that the therapeutic activity of these compounds could be primarily due to their interaction with nucleic acids but detailed reports are not available. We here explore the interaction of these drugs with nucleic acids considering DNA and RNA as a potential therapeutic target. The interaction of RES and GEN has been analysed in buffered solution with DNA [saline sodium citrate (SSC)] and RNA [tris ethylene diammine tetra acetic acid (TE)] using UV-absorption and Fourier transform infrared (FTIR) spectroscopy. The UV analysis revealed lesser binding affinity with nucleic acids at lower concentration of RES (P/D = 5.00 and 10.00), while at higher drug concentration (P/D = 0.75, 1.00 and 2.50) hyperchromic effect with shift in the ${\lambda}_{max}$ is noted for DNA and RNA. A major RES-nucleic acids complexes was observed through base pairs and phosphate backbone groups with K = $35.782\;M^{-1}$ and K = $34.25\;M^{-1}$ for DNA-RES and RNA-RES complexes respectively. At various concentrations of GEN (P/D = 0.25, 0.50, 0.75, 1.00 and 2.50) hyperchromicity with shift in the ${\lambda}_{max}$ from 260 $\rightarrow$ 263 om and 260 $\rightarrow$ 270 nm is observed for DNA-GEN and RNA-GEN complexes respectively. The binding constant (from UV analysis) for GEN-nucleic acids complexes could not be obtained due to GEN absorbance overlap with that of nucleic acids at 260 nm. Nevertheless a detailed analysis with regard to the interaction of these drugs (RES/GEN) with DNA and RNA could feasibly be understood by FTIR spectroscopy. The NH band of free DNA and RNA which appeared at $3550-3100\;cm^{-1}$ and $3650-2700\;cm^{-1}$ shifted to $3450-2950\;cm^{-1}$ and $3550-3000\;cm^{-1}$ in DNA-RES and RNA-RES complexes respectively. Similarly shifts corresponding to $3650-3100\;cm^{-1}$ and $3420-3000\;cm^{-1}$ have been observed in DNA-GEN and RNA-GEN complexes respectively. The observed reduction in NH band of free nucleic acids upon complexation of these drugs is an indication of the involvement of the hydroxyl (OH) and imino (NH) group during the interaction of the drugs and nucleic acids (DNA/RNA) through H-bonded formation. The interaction of RES and GEN with bases appears in the order of G $\geq$ T > C > A and A > C $\geq$ T > G. Further interaction of these natural compounds with DNA and RNA is also supported by changes in the vibrational frequency (shift/intensity) in symmetrical and asymmetrical stretching of aromatic rings of drugs in the complex spectra. No appreciable shift is observed in the DNA and RNA marker bands, indicating that the B-DNA form and A-family conformation of RNA are not altered during their interaction with RES and GEN.

Model verification and assessment of shear-flexure interaction in pile foundations

  • Lemnitzer, Anne;Nunez, Eduardo;Massone, Leonardo M.
    • Earthquakes and Structures
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    • v.11 no.1
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    • pp.141-163
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    • 2016
  • Fiber models have been developed and applied to various structural elements such as shear walls, beams and columns. Only scarcely have fiber models been applied to circular foundation systems such as cast in drilled holes shafts (CIDH). In pile foundations with constraint head boundary conditions, shear deformations can easily contribute to the lateral pile response. However, soil structure interaction formulations such as the p-y method, commonly used for lateral pile design, do not include structural shear deformations in its traditional derivation method. A fiber model that couples shear and axial-bending behavior, originally developed for wall elements was modified and validated on circular cross sections (columns) before being applied to a 0.61 m diameter reinforced concrete (RC) pile with fixed head boundary conditions. The analytical response was compared to measured test results of a fixed head test pile to investigate the possible impact of pile shear deformations on the displacement, shear, and moment profiles of the pile. Results showed that shear displacements and forces are not negligible and suggest that nonlinear shear deformations for RC piles should be considered for fixed-head or similar conditions. Appropriate sensor layout is recommended to capture shear deformation when deriving p-y curves from field measurements.

Interaction of Porcine Myofibrillar Proteins and Various Gelatins: Impacts on Gel Properties

  • Noh, Sin-Woo;Song, Dong-Heon;Ham, Youn-Kyung;Kim, Tae-Kyung;Choi, Yun-Sang;Kim, Hyun-Wook
    • Food Science of Animal Resources
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    • v.39 no.2
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    • pp.229-239
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    • 2019
  • The objectives of this study were to determine the interaction between porcine myofibrillar proteins and various gelatins (bovine hide, porcine skin, fish skin, and duck skin gelatins) and their impacts on gel properties of porcine myofibrillar proteins. Porcine myofibrillar protein was isolated from pork loin muscle (M. longissimus dorsi thoracis et lumborum). Control was prepared with only myofibrillar protein (60 mg/mL), and gelatin treatments were formulated with myofibrillar protein and each gelatin (9:1) at the same protein concentration. The myofibrillar protein-gelatin mixtures were heated from $10^{\circ}C$ to $75^{\circ}C$ ($2^{\circ}C/min$). Little to no impacts of gelatin addition on pH value and color characteristics of heat-induced myofibrillar protein gels were observed (p>0.05). The addition of gelatin slightly decreased cooking yield of heat-induced myofibrillar protein gels, but the gels showed lower centrifugal weight loss compared to control (p<0.05). The addition of gelatin significantly decreased hardness, cohesiveness, gumminess, and chewiness of heat-induced myofibrillar gels. Further, sodium dodecyl poly-acrylamide gel electrophoresis (SDS-PAGE) showed no interaction between myofibrillar proteins and gelatin under non-thermal conditions. Only a slight change in the endothermic peak (probably myosin) of myofibrillar protein-gelatin mixtures was found. The results of this study show that the addition of gelatin attenuated the water-holding capacity and textural properties of heat-induced myofibrillar protein gel. Thus, it could be suggested that well-known positive impacts of gelatin on quality characteristics of processed meat products may be largely affected by the functional properties of gelatin per se, rather than its interaction with myofibrillar proteins.

HEMATOLOGICAL RESPONSE OF SAUDI ARABIAN FOWL TO PROTEIN REARING REGIMENS

  • Alsobayel, A.A.;Attia, F.M.;Bayoumi, M.S.;Haroun, I.Y.
    • Asian-Australasian Journal of Animal Sciences
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    • v.3 no.2
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    • pp.107-114
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    • 1990
  • The purpose of this investigation was to study the hematological response of Saudi Arabian Baladi fowl to protein rearing regimens. Males and females were subjected to the following 4 protein rearing regimens: conventional, C; reverse protein, RP; 2 single-stage low protein, $SS_1$ and $SS_2$ using 15% and 12% CP diets, respectively. Regimen effect was highly significant ($$p{\leq_-}.01$$) on BW, PCY, TP and U-Ac and significant ($$p{\leq_-}.05$$) on TL. Serum chol levels were not affected by regimen. In general $SS_{2}$ birds showed the lowest values for all parameters studied, except for PCV. However, the differences were not significant in each case. Age and sex effects were highly significant ($$p{\leq_-}.01$$) for all parameters, however, the regimen X sex interaction was not significant except for PCV. Regimen X age interaction, on the other hand, was highly significant ($$p{\leq_-}.01$$) only for BW, TP and U-Ac concentrations. The data may suggest that low levels of protein in the rearing regimen is an important factor influencing levels of the blood parameters studied. The data also indicate a lack of clear relationship between hen-day egg production and the blood parameters studied.

An Isothermal Titration Microcalorimetric Study on the Interaction of Three Water-Soluble Porphyrins with Histone H2B

  • Bordbar, A.K.;Ghaderi, A.R.;Safaei, E.;Tangestaninejad, S.;Eslami, A.;Saboury, A.A.;Moosavi Movahedi, A.A.
    • Bulletin of the Korean Chemical Society
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    • v.24 no.5
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    • pp.547-551
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    • 2003
  • In the present work, the interaction of three water soluble porphyrins, tetra(p-trimethyle) ammonium phenyl porphyrin iodide (TAPP) as a cationic porphyrin, tetra sodium meso-tetrakis (p-sulphonato phenyle) porphyrin (TSPP) as an anionic porphyrin and manganese tetrakis (p-sulphonato phenyl) porphinato acetate (MnTSPP) as a metal porphyrin, with histone H₂B have been studied by isothermal titration microcalorimetry at 8 mM phosphate buffer, pH 6.8 and 27 °C. The values of binding constant, entropy, enthalpy and Gibbs free energy changes for binding of the first MnTSPP, and first and second TSPP and TAPP molecules were estimated from microcalorimetric data analysis. The results represent that the process is both entropy and enthalpy driven and histone induces self-aggregation of the porphyrins. The results indicate that both columbic and hydrophobic interactions act as self-aggregation driving forces for the formation of aggregates around histone.

Structural Insights into the Interaction of Terpenoids with Streptomyces avermitilis CYP107P2

  • Eunseo Jeong;Vitchan Kim;Changmin Kim;Yoo-bin Lee;Donghak Kim
    • Biomolecules & Therapeutics
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    • v.32 no.4
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    • pp.474-480
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    • 2024
  • Streptomyces avermitilis genome includes 33 genes encoding monooxygenation-catalyzing cytochrome P450 enzymes. We investigated the structure of CYP107P2 and its interactions with terpenoid compounds. The recombinant CYP107P2 protein was expressed in Escherichia coli and the purified enzyme exhibited a typical P450 spectrum upon CO-binding in its reduced state. Type-I substrate-binding spectral titrations were observed with various terpenoid compounds, including α-pinene, β-pinene, α-terpinyl acetate, and (+)-3-carene. The calculated binding affinities (Kd) ranged from 15.9 to 50.8 µM. The X-ray crystal structure of CYP107P2 was determined at 1.99 Å resolution, with a well-conserved overall P450 folding conformation. The terpenoid compound docking models illustrated that the structural interaction between monoterpenes and CYP107P2, with the distance between heme and terpenes ranging from 3.4 to 5.4 Å, indicates potential substrate binding for P450 enzyme. This study suggests that CYP107P2 is a Streptomyces P450 enzyme capable of catalyzing terpenes as substrates, signifying noteworthy advancements in comprehending a novel P450 enzyme's involvement in terpene reactions.

In Vitro Assessment of Cytochrome P450 Inhibition by Ambroxol and Cetirizine (암브록솔과 세티리진의 Cytochrome P450 저해 활성 평가)

  • Kim, Bong-Hee;Ryu, Chang Seon;Jang, Him Chan;Lee, Sang Yoon;Lee, Ji-Yoon;Chae, Jung-Woo;Kwon, Kwang-Il;Kim, Sang Kyum
    • YAKHAK HOEJI
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    • v.57 no.3
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    • pp.194-198
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    • 2013
  • In the present study we evaluated drug-drug interaction potential of ambroxol and cetirizine mediated by inhibition of CYP isoforms including CYP1A2, CYP2A6, CYP2B6, CYP2C9, CYP2C19, CYP2D6, CYP2E1 and CYP3A4 using pooled human liver microsomes (HLMs). As measured by liquid chromatography-electrospray ionization tandem mass spectrometry, cetirizine and ambroxol inhibited significantly CYP2E1 but the maximal inhibition was approximately 36% at 10 ${\mu}M$ cetirizine and 28% at 3 ${\mu}M$ ambroxol. In addition, CYP2D6 activity was decreased to approximately 83% of control activity in pooled HLM incubated with 3 ${\mu}M$ ambroxol. Activities of CYP1A2, CYP2A6, CYP2B6, CYP2C9, CYP2C19, and CYP3A4 were not significantly inhibited by cetirizine and ambroxol. Considering their maximal plasma concentration in human ($C_{max}$ of cetirizine is approximately 0.67 ${\mu}M$ and $C_{max}$ of ambroxol is 0.044 ${\mu}M$), these two drugs have very low possibility in drug-drug interaction by CYP inhibition in clinical situations.

Estimation of Genetic and Environmental Parameters of Carcass Traits in Hanwoo (Korean Native Cattle) Populations

  • Baik, D.H.;Hoque, M.A.;Choe, H.S.
    • Asian-Australasian Journal of Animal Sciences
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    • v.15 no.11
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    • pp.1523-1526
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    • 2002
  • Genetic parameters of carcass weight (CWT), dressing percent (DP), cook loss (CL), eye muscle area (EMA), back fat thickness (BFT), and meat tenderness in terms of mastication (MAS), shear force (SFR) and penetration (PEN) in Korean native cattle were estimated in this study. Effects of sire, location and their interaction on these traits were also evaluated. Sire effects were found to be significant on all the traits studied except for PEN. The CWT and DP were also significantly affected both by location (p<0.01) and by interaction effect between sire${\times}$location (p<0.05). The EMA was significantly (p<0.05) affected by location but not by interaction effect between sire${\times}$location. All the traits were positively correlated ($r_g$ and $r_p$) with each other except between CL and meat tenderness (negatively correlated). Moderate to high genetic correlations between CWT and other important traits were obtained; indicating that selection for CWT would lead to improve carcass quality. Heritability estimates were 0.64, 0.52, 0.37, 0.25, 0.19 and 0.18 for MAS, SFR, CWT, PEN, DP and EMA, respectively.

INTERACTION BETWEEN THREE MOVING GRIFFITH CRACKS AT THE INTERFACE OF TWO DISSIMILAR ELASTIC MEDIA

  • Das, S.;Patra, B.;Debnath, L.
    • Journal of applied mathematics & informatics
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    • v.8 no.1
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    • pp.59-69
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    • 2001
  • The paper deals with the interaction between three Griffith cracks propagating under antiplane shear stress at the interface of two dissimilar infinite elastic half-spaces. The Fourier transform technique is used to reduce the elastodynamic problem to the solution of a set of integral equations which has been solved by using the finite Hilbert transform technique and Cooke’s result. The analytical expressions for the stress intensity factors at the crack tips are obtained. Numerical values of the interaction efect have been computed for and results show that interaction effects are either shielding or amplification depending on the location of each crack with respect to other and crack tip spacing. AMS Mathematics Subject Classification : 73M25.

Spectroscopic Studies on the Interaction of N-alkyl Phenothiazines with Bovine Serum Albumin

  • Seetharamappa, J.;Shaikh, S.M.T;Kamat, B.P.
    • Journal of Photoscience
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    • v.12 no.1
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    • pp.25-32
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    • 2005
  • Binding of N-Alkyl phenothiazines (NAP) to bovine serum albumin (BSA) was studied by spectroscopic methods.It was found that the phenothiazine ring common to all drugs makes major contribution to interaction. However, the nature of alkylamino group at position 10 influences the protein binding significantly. Stern-Volmer plots indicated the presence of static component in the quenching mechanism. The high magnitude of rate constant of quenching indicated that the process of energy transfer occurs by intermolecular interaction and thus the drug-binding site is in close proximity to tryptophan residues of BSA. Binding studies in presence of hydrophobic probe, 8-anilino-1-naphthalein-sulphonic acid showed that there is hydrophobic interaction between drug and the probe and they do not share common sites in BSA. Thermodynamic parameters obtained from data at different temperatures showed that the binding of NAP to BSA predominantly involve hydrophobic forces. The effects of some cations and anions common ions were investigated on NAP-BSA interactions. The CD spectrum of BSA in presence of drug showedthat binding of drug leads to change in the helicity of the protein.

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