Hamzeh Amiri, Leila Moazzeni,
Volume 3, Issue 1 (6-2016)
Abstract
In order to study the interaction effects of salinity and ascorbic acid on the photosynthetic pigments, soluble sugar, proline, and protein in Satureja khuzestanica plant, factorial experiment was conducted in a completely randomized design (salinity in 4 levels 0, 40, 80 and 120g in 100kg soil and ascorbic acid in 2 levels 0 and 2 mM ) with 6 replicates. The results showed that salt stress reduced photosynthetic pigments amount by increasing the soil salinity from 0 to 40g NaCl in 100kg soil and then increased by 80g NaCl in 100kg soil and again decreased by concentration of 120g NaCl in 100kg soil. The amount of solouble sugar, proline and protein by the soil salinity increased from 0 to 40g in 100kg soil and then decreased in concentration of 80g NaCl in 100kg soil, in 120g NaCl in 100 kg soil increased amount of characters. In present of ascorbic acid photosynthetic pigments amount of pigments increased by increase the soil salinity from 0 to 40g NaCl in 100kg soil and then decreased by 80g NaCl in 100kg soil and again increased by concentration of 120g NaCl in 100kg soil. But, amount of solouble sugar, proline and protein by the soil salinity decreased from 0 to 40g in 100kg soil and then increased in concentration of 80g NaCl in 100kg soil. Finally, in 120g NaCl in 100kg soil decreased amount of characters.
Golnaz Parvizi Fard, Lale Solouki, Mostafa Zakariazadeh, Hossein Haghaei, Somaieh Soltani,
Volume 9, Issue 3 (12-2022)
Abstract
Human serum albumin is one of the most important blood proteins that has the ability to bind a wide range of compounds and different drugs. Hence, knowing how drugs bind to albumin is crucial to understand their pharmacokinetics and pharmacodynamic properties. The binding of drugs to protein affects the drug's excretion, distribution and interaction in the target tissues. Nicotinamide (NA) is a safe and inexpensive medical supplement that used to prevent and treat vitamin B3 deficiency. In this research, the molecular mechanism of the interaction between nicotinamide and human serum albumin was studied by the utilization of spectroscopic and molecular docking methods. The effects of temperature, acidic/basic pHs, metal ions, urea, and glucose on the interaction between nicotinamide and human serum albumin were also investigated. The spectroscopic studies indicated that the interaction between nicotinamide and human serum albumin is mainly controled by hydrophobic forces and the interaction is spontaneous. The number of binding site and binding constant is 1 and 4.6×104 (L/mol), respectively, which were increased in the presence of glucose. The presence of metallic ions and basic pH decreased the binding constant of nicotinamide to albumin. The obtained results indicated that nicotinamide tend to binds to the similar sites wherever the molecules with acidic moieties bind. The results could be helpful to interpret the mechanisms of actions of nicotinamide in the various physiological phenomena in the human body.
