Docking against Lung cancer protein and Drug-likeliness of Bioactive Compounds from Phymatosorus scolopendria (Burm.F.) Pic. Serm.

Phymatosorus scolopendria (Burm.F.) Pic. Serm. is a medicinally important fern which is used traditionally by various people all over the World. The aim of this research focuses on the docking against lung cancer protein (2ITO) with bioactive compounds of Phymatosorus scolopendria (Burm.F.) Pic. Serm. which is obtained by using Gas Chromatography Mass Spectroscopy. The same compounds were analysed using Lipinski’s rule of five for its pharmacological prediction. The bioactive compounds were further referred for ADMET property to find its pharmacokinetic potency and prediction towards its potential as drug in future. Among the four compounds docked with the Lung cancer protein (2ITO) 4-Nitrophenyl laurate shows high docking score followed by Hexadecanoic acid, 4 Nitrophenyl ester and Myristic acid Vinyl ester. Out of four compounds studied three compounds satisfied the drug-likeliness based on Lipinski’s rule of five. The present work suggests the bioactive compounds of Phymatosorus scolopendria (Burm.F.) Pic. Serm. for further in vitro and in vivo studies for its anticancer benefits especially related to lung cancer.

Further Stabilization of Alcalase Immobilized on Glyoxyl Supports: Amination Plus Modification with Glutaraldehyde

Alcalase was immobilized on glyoxyl 4% CL agarose beads. This permitted to have Alcalase preparations with 50% activity retention versus Boc-l-alanine 4-nitrophenyl ester. However, the recovered activity versus casein was under 20% at 50 °C, as it may be expected from the most likely area of the protein involved in the immobilization. The situation was different at 60 °C, where the activities of immobilized and free enzyme became similar. The chemical amination of the immobilized enzyme or the treatment of the enzyme with glutaraldehyde did not produce any significant stabilization (a factor of 2) with high costs in terms of activity. However, the modification with glutaraldehyde of the previously aminated enzyme permitted to give a jump in Alcalase stability (e.g., with most than 80% of enzyme activity retention for the modified enzyme and less than 30% for the just immobilized enzyme in stress inactivation at pH 7 or 9). This preparation could be used in the hydrolysis of casein at pH 9 even at 67 °C, retaining around 50% of the activity after 5 hydrolytic cycles when the just immobilized preparation was almost inactive after 3 cycles. The modified enzyme can be reused in hydrolysis of casein at 45 °C and pH 9 for 6 cycles (6 h) without any decrease in enzyme activity.