Enzymatic Activity Enhancement of Non-Covalent Modified Superoxide Dismutase and Molecular Docking Analysis

Abstract

The enzyme activity of superoxide dismutase was improved in the pyrogallol autoxidation system by about 27%, after interaction between hydroxypropyl-β-cyclo- dextrin and superoxide dismutase. Fluorescence spectrometry was used to study the interaction between hydroxypropyl-β-cyclodextrin and superoxide dismutase at different temperatures. By doing this, it can be found that these interactions increase fluorescence sensitivity. In the meantime, the synchronous fluorescence intensity revealed the interaction sites to be close to the tryptophan (Trp) and tyrosine (Tyr) residues of superoxide dismutase. Furthermore, molecular docking was applied to explore the binding mode between the ligands and the receptor. This suggested that HP-β-CD interacted with the B ring, G ring and the O ring and revealed that the lysine (Lys) residues enter the nanocavity. It was concluded that the HP-β-CD caused specific conformational changes in SOD by non-covalent modification.

Antioxidant Activity Evaluation of FlexirubinType Pigment from Chryseobacterium artocarpi CECT 8497 and Related Docking Study

“…The superoxide anion radical is an inevitable and cytotoxic byproduct of aerobic metabolism. Superoxide dismutases (SODs) metalloenzyme act as defense systems in all aerobes to avoid ROS’s extensive production, catalyze superoxide radicals’ disproportionation to hydrogen peroxide (H 2 O 2 ) and molecular oxygen (O 2 )through oxidation and reduction alternation process [ 17 ]. SOD can also be used as an additional parameter for diagnosing oxidative stress-related disease [ 18 ].…”

Biomimetic Membrane-Structured Nanovesicles Carrying a Supramolecular Enzyme to Cure Lung Cancer

“…First, Aase was taken into hydroxypropyl-β-cyclodextrin (HPCD) to self-assemble into the HPCD-Aase supramolecular amphiphile (AS) via noncovalent reversible interactions . The combination of Aase in HPCD may increase and maintain enzymatic activity by providing support to hold the enzyme, preventing degradation from the external environment, avoiding aggregation of the Aase molecule, and causing specific favorable conformational changes in Aase, similar to the actions of other sole cyclodextrin-enzymes (poly-β-cyclodextrin-organophosphorus hydrolase, HPCD-superoxide dismutase, and HPCD-lysozyme). In addition to acting as an excipient, HPCD acts as an antitumor agent by modifying cholesterol accumulation and dysregulating cholesterol metabolism in various malignancies …”

Uricase alkaline enzymosomes with enhanced stabilities and anti-hyperuricemia effects induced by favorable microenvironmental changes

“…Fluorescence changes of UCU (in the absence or presence of CAT) or its ESU (or ESUC) in buffer-A to -D were determined according to a modified enzyme fluorescence method 46 47 . Briefly, UCU (50 μg/mL) or UCU in the presence of CAT (i.e., the mixture of 25 μg/mL UCU and 25 μg/mL CAT) was separately determined.…”

“…The mixtures were placed at 37 °C for 1 h, and then subjected to centrifugation at 3000 rpm for 10 min. Then, the supernatant was taken out and determined at 540 nm 46 . The hemolysis rate was calculated by comparing the absorbance of the sample to that of distilled water.…”