ArticlePloS one2021
Prediction of hyaluronic acid target on sucrase-isomaltase (SI) with reverse docking and molecular dynamics simulations for inhibitors binding to SI.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- Theoretical Studies for the Discovery of Potential Sucrase-Isomaltase Inhibitors from Maize Silk Phytochemicals: An Approach to Treatment of Type 2 Diabetes.Molecules (Basel, Switzerland) · 2023Article
- Extraction Efficiency and Alpha-Glucosidase Inhibitory Activities of Green Tea Catechins by Different Infusion Methods.Foods (Basel, Switzerland) · 2023Article
- Interspecies hybridization betweenFrontiers in microbiology · 2023Article
- Atomic-Resolution Experimental Structural Biology and Molecular Dynamics Simulations of Hyaluronan and Its Complexes.Molecules (Basel, Switzerland) · 2022Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Auricularia cornea (E.) polysaccharide is an important component of A. cornea Ehrenb, a white mutant strain of Auricularia with biological activities, such as enhancement of human immune function and cancer prevention. The hyaluronic acids (HAs) are important components of the A. cornea polysaccharide and have extremely high medicinal value. In this study, we used HA to search the target protein sucrase-isomaltase (SI). In addition, we also performed molecular dynamics (MD) simulations to explore the binding of three inhibitors (HA, acarbose and kotalanol) to SI. The MD simulations indicated that the binding of the three inhibitors may induce the partial disappearance of α helix in residues 530-580. Hence, the hydrogen bond for Gly570-Asn572, which was near the catalytic base Asp471 in SI, was broken during the binding of the three inhibitors. We reveal a new inhibitor for SI and provide reasonable theoretical clues for inhibitor binding to SI.
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