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"Wang, Yigui"

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Wang, E. Z., & Wang, Y. (2020). Computational study in a PUI using XSEDE resources and ECSS support. ACM International Conference Proceeding Series, 534–537. https://doi.org/10.1145/3311790.3400849

In the past 5 years, we have been using XSEDE resources and ECSS support to conduct research at Southern Connecticut State University (SCSU), a primary undergraduate institution (PUI). First, the regioselectivity was successfully investigated in the synthesis of 5-FU derivatives with phase transition method and silver salt method; then the Hard and Soft Acids and Bases (HSAB) principle and the Marcus theory were unified in the study of ambident reactivity; at last our research was expanded from reactions of molecules to reactions on the solid surface. We would like to share our results and emphasize the importance of XSEDE resources and ECSS support for the research in PUIs. © 2020 ACM.

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Gambardella, M. D., Wang, Y., & Pang, J. (2025). Molecular Dynamics Studies on the Inhibition of Cholinesterases by Secondary Metabolites. Catalysts, 15(8). https://doi.org/10.3390/catal15080707

The search for selective anticholinergic agents stems from varying cholinesterase levels as Alzheimer’s Disease progresses from the mid-to-late stage and from butyrylcholinesterase’s (BChE) role in β-amyloid plaque formation. While structure-based and pharmacophore-based virtual screening could search from large libraries in a short time, these methods do not consider dynamic features that result from a ligand’s inhibition of the enzyme and consequently may under- or overexaggerate enzyme selectivity of a given ligand. In this computational study, we probed the selectivity of representative secondary metabolite compounds against acetylcholinesterase and BChE through molecular dynamics simulations. The results were evaluated by analysis of the root mean squared deviation of ligand heavy atoms, the radius of gyration of each inhibited and uninhibited enzyme, root mean squared fluctuation of residues, intermolecular interaction energy, and linear interaction energy approximation of the Gibbs free energy of binding. These considerations further reveal the induced-fit characteristics contributing to ChE selectivity that are predominantly due to the greater flexibility of BChE’s active site gorge. © 2025 by the authors.
Gambardella, M. D., Wang, Y., & Pang, J. (2025). The Selectivity of Butyrylcholinesterase Inhibitors Revisited. Molecules, 30(21). https://doi.org/10.3390/molecules30214201

Acetylcholinesterase (AChE) inhibitors are the primary target for single-molecule anti-Alzheimer’s disease (AD) therapeutics. Though AChE has historically been the focus of investigation for small-molecule inhibitors, interest in another cholinergic enzyme, butyrylcholinesterase (BChE), has grown in recent years. Attention stems from BChE’s role in β-amyloid (Aβ) protein aggregation and an increase in BChE concentration during the late stages of AD, where a decrease in AChE concentration is also observed. Currently, five FDA-approved drugs are on the market for inhibiting AChE, though no BChE-selective drugs have been approved so far. In this review, we focus on newly identified BChE selective inhibitors and present the ideas behind these discoveries. © 2025 by the authors.

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