β-Galactosidase inhibition explored by biochemical methods and in silico 1 studies for plant polyphenols
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Date
Journal Title
Journal ISSN
Volume Title
Publisher
Academic Press Inc.
Series Info
Archives of Biochemistry and Biophysics; 25 July 2025, 110568
Scientific Journal Rankings
Abstract
β-Galactosidase is a lysosomal enzyme whose deficiency is associated with genetic disorders such as GM1 gangliosidosis, prompting the search for novel enzyme modulators with therapeutic potential. The current study evaluated the inhibitory potential of selected natural polyphenols against β-galactosidase using a combined approach of biochemical assays and computational modeling. Sixteen plant-derived compounds were initially screened through molecular docking against Aspergillus oryzae β-galactosidase. Among these, hesperidin, rutin, and chlorogenic acid exhibited the most favorable interactions and were subsequently assessed through in vitro enzyme inhibition assays and MM/GBSA binding energy calculations. These compounds showed potential inhibitory effects and stable binding within the enzyme’s active site. Although classical pharmacological chaperone activity was not directly demonstrated, the observed modulation of enzyme function suggests potential for further development of these polyphenols as structurally distinct glycosidase inhibitors. The findings provide a basis for future investigations aimed at natural product-based strategies to manage lysosomal storage disorders such as GM1 gangliosidosis.
Description
SJR 2024
0.912 Q1
H-Index
198
Citation
Zayed, A., Sayah, K., Sharma, K., Radwan, R. A., & Ezzat, S. M. (2025). β-Galactosidase inhibition explored by biochemical methods and in silico studies for plant polyphenols. Archives of Biochemistry and Biophysics, 110568. https://doi.org/10.1016/j.abb.2025.110568