H.A. Tajmir-Riahi

TL;DR: Examination of the interaction of human serum albumin with quercetin, kaempferol and delphinidin in aqueous solution at physiological conditions showed that flavonoids are located along the polypeptide chains through H-bonding interactions with overall affinity constant, and major reduction of HSA α-helix is indicative of a partial protein unfolding upon flavonoid interaction.

TL;DR: Results revealed that the binding of serum albumins with chitosan nanoparticles induces a significant change in protein morphology and the shape of the polymer.

TL;DR: The protein conformation was altered with major reduction of α-helix from 60 to 55% to 40 to 40% and increase of β-structure from 22 to 15% (free HSA) to 33 to 23% in the drug- Protein secondary, structure are attributed to partial, unfolding of HSA on drug complexation.

TL;DR: The results show intercalated flavonoids can make them strong antioxidants to protect DNA from harmful free radical reactions, and a partial B to A-DNA transition occurs at high drug concentration, while tRNA remains in A-family structure.

TL;DR: The antioxidant activity of CRT, DMCRT and safranal was tested by the DPPH (2,2-diphenyl-1-picrylhydrazyl) antioxidant activity assay and their IC(50) values were compared to that of well known antioxidants such as Trolox and Butylated Hydroxy Toluene (BHT).