Study on the interaction of hyaluronidase with certain flavonoids

Chitosan as a Functional Carrier for the Local Delivery Anti-Inflammatory Systems Containing Scutellariae baicalensis radix Extract

“…Using computational modeling approaches, it was possible to demonstrate that hydrophobic interaction, electrostatic force, and hydrogen bond are the main interaction forces between baicalin and hyaluronidase. The results show that the binding leads to changes in the secondary structure of the enzyme [ 31 ]. A significant increase in the anti-inflammatory effect, including the inhibition of the degradation of hyaluronic acid, indicates the combined effect of active compounds from S. baicalensis extract, particularly baicalin and baicalein [ 32 ].…”

“…It was also proven that the degree of deacetylation is a statistically significant variable impacting the IC 50 in the case of anti-hyaluronidase activity ( Figure 6 b). The mechanism of inhibiting the activity of hyaluronidase may be related to the interaction of an increasing number of −NH 2 groups with an increase in the deacetylation degree, which may lead to changes in the secondary structure of the enzyme [ 31 ]. Thus, a considerable increase in the inhibition of hyaluronic acid degradation may point toward a combined effect of active compounds from S. baicalensis extract, particularly baicalein and chitosan molecules [ 39 ].…”

Isolation, Characterization, Genome Annotation, and Evaluation of Hyaluronidase Inhibitory Activity in Secondary Metabolites of Brevibacillus sp. JNUCC 41: A Comprehensive Analysis through Molecular Docking and Molecular Dynamics Simulation

“…Furthermore, the fluctuation in docking binding energies The docking results reveal several key interactions: Firstly, the carbonyl group of methyl indole-3-acetate forms hydrogen bonds with Tyr-247, a residue recognized for stabilizing oxidation during transition state formation [49], and the amino group interacts with Tyr-75 via hydrogen bonding. Secondly, the phenyl group interacts with Tyr-202, a hydrophobic amino acid likely involved in substrate binding [84], via π-π stacking and π-alkyl interactions. Thirdly, interactions occur between the compound and hydrophobic amino acid residues, specifically Asp-129 and Glu-131, recognized for their chemical catalysis role [48], forming π-anion and carbon-hydrogen interactions, respectively.…”

Study of the interaction mechanism of silver nanoparticles with γ-globulin, fibrinogen and hyaluronidase

“…The CD spectrum of HAase has negative peaks at 205 nm and 223 nm, indicating that HAase may be the (a + b) class of protein. [63][64][65] The absolute value of the negative value at 205 nm becomes smaller upon the addition of AgNPs with a slight red shift in the wavelength, indicating a decrease in the a-helix content of HAase upon AgNP binding. This clearly indicates that the ordered structures in g-globulin (b-sheet), fibrinogen (a-helix), and HAase (a-helix) are reduced and the disordered structures are increased.…”