4 research outputs found

    High dilutions of two drugs induce changes in crystal water structure of lactose as revealed by thermogravimetry and differential scanning calorimetry

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    Ultra-high dilutions (UHD) of drugs used in homeopathy are preserved in sugars. How do solid sugars assimilate characteristics of UHDs? This study attempts to answer this question. The three UHDs of Acid fluoric, Acid nitric, and ethanol were mixed with lactose at 1 µL/g and analyzed by thermogravimetry (TG) and differential scanning calorimetry (DSC) to see any change in their crystal water. TG results show a mass loss of 4.9% at 146.8C for Acid fluoric 30 cH, of 7.1% at 146.6C for Acid nitric 30 cH, and5.1% at 146.5C for ethanol. DSC results show that the change in enthalpy for Acid fluoric 30 cH is 157.3 J/g at 153.8C, that for Acid nit 30 cH is 122.8 J/g at 148.3C, and that for ethanol is 154.9 J/g at 156.3C. Bound water in lactose crystals and corresponding enthalpies vary markedly in the three drugs tested. This indicates that the number of hydrogen bonds and their bond strength vary inbound water of medicated lactose crystals

    Cannabis as homeopathic medicine in extreme dilutions: Thermal analysis for their differentiation and action on a protein

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    506-513Cannabis indica and C. sativa have been used in homeopathy in extreme dilutions, called potencies, for therapeutic purposes since 1841. The purpose of the present study is to see whether Cannabis dilutions have specific levels of free water molecules which characterize other homeopathic potencies. The second objective is to see whether Cannabis mother tincture (MT) and potencies act on the binding sites of a protein. The three potencies 8, 14 and 32 cH were prepared from Cannabis mother tincture (MT) by successive dilution followed by succussion in 8, 14 and 32 steps, respectively. The 3 potencies of diluent medium 90% EtOH were similarly prepared. Each potency was analysed by differential scanning calorimetry (DSC) to determine the free water level in it. The drug potencies and unpotentised EtOH were tested for their binding reaction with a protein human serum albumin (HSA) by isothermal calorimetry (ITC). MTs and the potencies differ from each other and also from water control and EtOH with respect to free water content as revealed by DSC. MTs, their potencies and EtOH bind to HSA showing difference in thermodynamic parameters in terms of stoichiometry, binding constant, change in enthalpy, entropy and Gibbs free energy. Potencies may initiate their individual effect through binding with a protein thereby leading to subsequent biochemical events inside the cell

    Cannabis as homeopathic medicine in extreme dilutions: Thermal analysis for their differentiation and action on a protein

    Get PDF
    Cannabis indica and C. sativa have been used in homeopathy in extreme dilutions, called potencies, for therapeutic purposes since 1841. The purpose of the present study is to see whether Cannabis dilutions have specific levels of free water molecules which characterize other homeopathic potencies. The second objective is to see whether Cannabis mother tincture (MT) and potencies act on the binding sites of a protein. The three potencies 8, 14 and 32 cH were prepared from Cannabis mother tincture (MT) by successive dilution followed by succussion in 8, 14 and 32 steps, respectively. The 3 potencies of diluent medium 90% EtOH were similarly prepared. Each potency was analysed by differential scanning calorimetry (DSC) to determine the free water level in it. The drug potencies and unpotentised EtOH were tested for their binding reaction with a protein human serum albumin (HSA) by isothermal calorimetry (ITC). MTs and the potencies differ from each other and also from water control and EtOH with respect to free water content as revealed by DSC. MTs, their potencies and EtOH bind to HSA showing difference in thermodynamic parameters in terms of stoichiometry, binding constant, change in enthalpy, entropy and Gibbs free energy. Potencies may initiate their individual effect through binding with a protein thereby leading to subsequent biochemical events inside the cell
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