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25 results on '"Meng, Fanhao"'

8. Detection of Aircraft Emissions Using Long-Path Differential Optical Absorption Spectroscopy at Hefei Xinqiao International Airport

Author

Duan, Jun, primary, Qin, Min, additional, Fang, Wu, additional, Liao, Zhitang, additional, Gui, Huaqiao, additional, Shi, Zheng, additional, Yang, Haining, additional, Meng, Fanhao, additional, Shao, Dou, additional, Hu, Jiaqi, additional, Han, Baobin, additional, Xie, Pinhua, additional, and Liu, Wenqing, additional

Published
2022
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14. Fragment-Based Structural Optimization of a Natural Product Itampolin A as a p38α Inhibitor for Lung Cancer

Author

Shan Wang, Meng Fanhao, Ming-Yang Wang, Jing-wei Liang, and Xin-yang Li

Subjects
p38α, Quantitative structure–activity relationship, Lung Neoplasms, Pharmaceutical Science, Antineoplastic Agents, Secondary metabolite, Article, Mitogen-Activated Protein Kinase 14, chemistry.chemical_compound, Inhibitory Concentration 50, Structure-Activity Relationship, itampolin A, Drug Discovery, medicine, Animals, Humans, novel inhibitor, Tyrosine, Pharmacology, Toxicology and Pharmaceutics (miscellaneous), IC50, lcsh:QH301-705.5, Cell Proliferation, Enzyme Assays, antitumor, A549 cell, Biological Products, Natural product, Molecular Structure, Total synthesis, Porifera, Molecular Docking Simulation, chemistry, Biochemistry, lcsh:Biology (General), A549 Cells, Drug Design, FBDD, Drug Screening Assays, Antitumor, Lead compound, medicine.drug
Abstract

Marine animals and plants provide abundant secondary metabolites with antitumor activity. Itampolin A is a brominated natural tyrosine secondary metabolite that is isolated from the sponge Iotrochota purpurea. Recently, we have achieved the first total synthesis of this brominated tyrosine secondary metabolite, which was found to be a potent p38α inhibitor exhibiting anticancer effects. A fragment-based drug design (FBDD) was carried out to optimize itampolin A. Forty-five brominated tyrosine derivatives were synthesized with interesting biological activities. Then, a QSAR study was carried out to explore the structural determinants responsible for the activity of brominated tyrosine skeleton p38α inhibitors. The lead compound was optimized by a FBDD method, then three series of brominated tyrosine derivatives were synthesized and evaluated for their inhibitory activities against p38α and tumor cells. Compound 6o (IC50 = 0.66 μM) exhibited significant antitumor activity against non-small cell lung A549 cells (A549). This also demonstrated the feasibility of the FBDD method of structural optimization.

Published
2019

20. A Comprehensive In Silico Method to Study the QSTR of the Aconitine Alkaloids for Designing Novel Drugs

Author

Qi Sun, Ming-Yang Wang, Kamara Mohamed Olounfeh, Meng Fanhao, Jing-Wei Liang, and Zhao Nan

Subjects
0301 basic medicine, Quantitative structure–activity relationship, In silico, Quantitative Structure-Activity Relationship, Pharmaceutical Science, Computational biology, Molecular Dynamics Simulation, alkaloids, Article, Analytical Chemistry, Protein–protein interaction, lcsh:QD241-441, 03 medical and health sciences, chemistry.chemical_compound, lcsh:Organic chemistry, Protein Interaction Mapping, Drug Discovery, Aconitine, heterocyclic compounds, quantitative structure–toxicity relationship (QSTR), Protein Interaction Maps, Physical and Theoretical Chemistry, String database, Cardiotoxicity, Organic Chemistry, Reproducibility of Results, Protein kinase II, Molecular Docking Simulation, 030104 developmental biology, chemistry, Chemistry (miscellaneous), Docking (molecular), Drug Design, docking, network, aconitine, Molecular Medicine
Abstract

A combined in silico method was developed to predict potential protein targets that are involved in cardiotoxicity induced by aconitine alkaloids and to study the quantitative structure&ndash, toxicity relationship (QSTR) of these compounds. For the prediction research, a Protein-Protein Interaction (PPI) network was built from the extraction of useful information about protein interactions connected with aconitine cardiotoxicity, based on nearly a decade of literature and the STRING database. The software Cytoscape and the PharmMapper server were utilized to screen for essential proteins in the constructed network. The Calcium-Calmodulin-Dependent Protein Kinase II alpha (CAMK2A) and gamma (CAMK2G) were identified as potential targets. To obtain a deeper insight on the relationship between the toxicity and the structure of aconitine alkaloids, the present study utilized QSAR models built in Sybyl software that possess internal robustness and external high predictions. The molecular dynamics simulation carried out here have demonstrated that aconitine alkaloids possess binding stability for the receptor CAMK2G. In conclusion, this comprehensive method will serve as a tool for following a structural modification of the aconitine alkaloids and lead to a better insight into the cardiotoxicity induced by the compounds that have similar structures to its derivatives.

Published
2018

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