Effect of chrysin omega-3 and 6 fatty acid esters on mushroom tyrosinase activity, stability, and structure.

The estreification of chrysin with α-Linolenic acid (complex I) and linoleic acid (complex II) poly unsaturated fatty acids resulted to design of new mushroom tyrosinase (MT) inhibitors. Thermodynamic parameters of enzymes, including the melting point (Tm ) and ∆G values, were obtained from thermal and chemical denaturation curves. Complexes I and II showed a competitive inhibitory effect on MT with Ki values of 0.45 and 0.29 mM, respectively. The Tm values were calculated as 328.6, 322.4, and 318 K and the ∆G values as 62.8, 52.9, and 47.1 KJ mol-1 for the enzyme alone and its interaction with complexes I and II, respectively. Intrinsic and extrinsic fluorescence techniques showed structural instability of the enzyme in concomitance with a decrease in the regular secondary structure acquired using CD spectrometry. This data clearly prove that the new derivatives show a stronger inhibitory effect than the separate compounds. Molecular docking analysis showed that the best possible interaction condition was achieved for chrysin with n-6. PRACTICAL APPLICATIONS: MT is a suitable model in medicine for the investigation of melanogenesis, skin disorders, and hyperpigmentation because of its accessibility and close structural similarity to mammalian tyrosinase. In recent years, the designing of tyrosinase inhibitors from natural substances for prevention of hyperpigmentation in medicine, skin cosmetics, and undesired browning in agriculture and food industry has risen sharply. Many of the pharmaceutical products based on the use of flavonoids and poly unsaturated acids as natural compounds or on their semi-synthetic derivatives have been interested for investigations because of their usefulness in many pathological conditions such as inflammation, cancer, and skin disorders. The limitation of the flavonoids applications are low bioavailability, permeability, and solubility for the cells. In this study, conjugation of chrysin with n-3 and n-6 fatty acids resulted in a stronger inhibitors of MT with a synergic inhibitory effect on its activity.

The effect of cupric and ferric ions on antioxidant properties of human serum albumi.

The interaction of both ferric (Fe³âº) and cupric (Cu²âº) ions with human serum albumin (HSA) was assayed at a temperature of 27°C in aqueous solution using isothermal titration calorimetry. The association equilibrium constant and the molar enthalpy for one binding is 1.7 × 105 M-1 and -31.37 kJ • M⁻¹, respectively. To obtain the binding parameters of metal ion-protein interaction over the whole range of Fe³âº concentrations, the extended solvation model was applied. The solvation parameters obtained from this model were attributed to the structural change of HSA. The binding parameters obtained from the extended solvation model indicate that the stability of HSA was decreased as a result of its binding with ferric ions, which cause dampening the antioxidant property of HSA. Cuperic ion increases the stability of HSA considerably, indicating that the antioxidant property of human serum albumin are increased as a result of its interaction with cupric ion.