Potential Effect of Baobab's Polyphenols as Antihyperlipidemic Agents: In Silico Study.

Adansonia digitata L. is an African tree commonly called baobab. This tree is effectively used in traditional medicine to treat cardiovascular disorders. Hyperlipidemia is a well-known cardiovascular risk factor associated with the increased incidence of mortality worldwide. This study aimed to demonstrate the mechanism of baobab polyphenols in the activities of hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase and pancreatic lipase as lipid metabolic enzymes. Molecular docking and an incentive for drug design showed that all the polyphenols in baobab bound to the proteins with higher affinity and a lower binding energy compared with simvastatin as the positive control (ΔG: from -5.5 kcal/mol to -6.5 kcal/mol). The same polyphenols exhibited a considerable binding affinity to pancreatic lipase (ΔG: from -7.5 kcal/mol to -9.8 kcal/mol) in comparison with the control and HMG-CoA reductase. Quercetin showed the best docking score from the selected Baobab polyphenols (ΔG = -9.8 kcal/mol). The root mean square deviation (RMSD) results indicated that stable epicatechin and quercetin complexes were demonstrated with HMG-CoA reductase, and other less stable complexes were developed using rutin and chlorogenic acid. Moreover, the analysis of the root mean square fluctuation (RMSF) simulation results was consistent with that of the RMSD. The RMSF value for all the baobab polyphenols, including the crystal control ligand, was kept between 0.80 and 8.00 Å, similarly to simvastatin, and less than 4.8 Å for pancreatic lipase. Chlorogenic acid, quercetin, epicatechin, and rutin had negative ΔG binding scores from highest to lowest. The same ligands displayed more negative ΔG binding scores than those observed in HMG-CoA reductase and crystal control ligand (methoxyundecyl phosphinic acid) in their simulation with pancreatic lipase. In conclusion, baobab polyphenols interact with HMG-CoA reductase and pancreatic lipase to inhibit their substrate binding and block their activity.

Structural stability and solubility of glycated camel lens ζ-crystallin.

The camel has several biochemical, physiological, and anatomical features to withstand the harsh desert climate. Camel eye lens contains a novel protein (ζ-crystallin) in bulk quantity. Previous reports suggest that non-enzymatic glycation of eye lens proteins plays an important role in the etiology of cataract. In this study, we have characterized the role of glucose, fructose, and methylglyoxal (MGO) in the glycation of camel lens ζ-crystallin. From the results obtained, it was found that MGO reacted rapidly, fructose reacted moderately, and glucose was the least reactive even after prolonged incubation (>100 days). Glycation with MGO and fructose led to changes in the structure of ζ-crystallin, while glucose had no remarkable effect. The surface hydrophobicity did not change and no aggregates or amyloid fibrils were observed in the glycated ζ-crystallin. Moreover, the secondary structure of glycated ζ-crystallin remained similar after glycation. Our results suggested that due to natural adaptation, the camel lens protein ζ-crystallin retained its structure and solubility even after glycation to perform the single known function of the lens proteins: to focus unscattered light on the retina.

Effect of cetyltrimethylammonium bromide (CTAB) on the conformation of a hen egg white lysozyme: A spectroscopic and molecular docking study.

The interactions between cetyltrimethylammonium bromide (CTAB) and hen egg white lysozymes (HEWL) was carried out to investigate protein-surfactant interaction mechanisms while both exist in the overall same charged state. The interactions between CTAB and the HEWL were examined with circular dichroism (CD), dynamic light scattering (DLS), fluorescence spectroscopy, and computational docking at a pH9.0 at room temperature. The far-UV CD and fluorescence results revealed that CTAB at concentrations from 0.15 to 10.0mM influenced the secondary as well as the tertiary structure of HEWL. The secondary structure of the HEWL was retained, while the tertiary structure of the HEWL was disrupted in the CTAB-treated samples at pH9.0. The hydrodynamic radii of the HEWL were also expanded in the presence of CTAB. Molecular docking studies showed that CTAB formed one electrostatic and four hydrophobic interactions, as well as one carbon hydrogen bond with HEWL. The data obtained from spectroscopic and computational studies demonstrated that the positively charged head and 18­carbon alkyl chain of the CTAB interacted through weak electrostatic and strong hydrophobic interactions.