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Your search keyword '"Xu, Tiefeng"' showing total 919 results
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919 results on '"Xu, Tiefeng"'

51. Carbonylative synthesis of 2-(trifluoromethyl)quinazolin-4(3H)-ones from trifluoroacetimidoyl chlorides and amines based on an activated carbon fiber supported palladium catalyst.

Author

Wang, Hui, Ling, Sihao, Xu, Tiefeng, and Chen, Zhengkai

Subjects
PALLADIUM catalysts, CATALYST supports, ACTIVATED carbon, HETEROGENEOUS catalysts, CHEMICAL properties, CARBON fibers, CARBON composites
Abstract

Activated carbon fibers, known for their unique physical and chemical properties, are increasingly utilized in diverse industries, including textiles and fabrics, and can serve as ideal supports of heterogeneous palladium catalysts. An efficient strategy for the preparation of 2-(trifluoromethyl)quinazolin-4(3H)-ones via a three-component carbonylative reaction of trifluoroacetimidoyl chlorides and amines using a heterogeneous activated carbon fiber-supported palladium catalyst has been developed. In contrast to the homogeneous catalytic protocol reported previously, the higher efficiency of the heterogeneous reaction is observed and the Pd/ACFs catalyst could be recycled five times with good stability and slightly decreased catalytic reactivity. [ABSTRACT FROM AUTHOR]

Published
2024
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67. Structure-Based Virtual Screening for Methyltransferase Inhibitors of SARS-CoV-2 nsp14 and nsp16.

Author

Wu, Kejue, Guo, Yinfeng, Xu, Tiefeng, Huang, Weifeng, Guo, Deyin, Cao, Liu, and Lei, Jinping

Subjects
SARS-CoV-2, MOLECULAR dynamics, DRUG development, ANTIVIRAL agents, COVID-19 pandemic, IDENTIFICATION
Abstract

The ongoing COVID-19 pandemic still threatens human health around the world. The methyltransferases (MTases) of SARS-CoV-2, specifically nsp14 and nsp16, play crucial roles in the methylation of the N7 and 2′-O positions of viral RNA, making them promising targets for the development of antiviral drugs. In this work, we performed structure-based virtual screening for nsp14 and nsp16 using the screening workflow (HTVS, SP, XP) of Schrödinger 2019 software, and we carried out biochemical assays and molecular dynamics simulation for the identification of potential MTase inhibitors. For nsp14, we screened 239,000 molecules, leading to the identification of three hits A1–A3 showing N7-MTase inhibition rates greater than 60% under a concentration of 50 µM. For the SAM binding and nsp10-16 interface sites of nsp16, the screening of 210,000 and 237,000 molecules, respectively, from ZINC15 led to the discovery of three hit compounds B1–B3 exhibiting more than 45% of 2′-O-MTase inhibition under 50 µM. These six compounds with moderate MTase inhibitory activities could be used as novel candidates for the further development of anti-SARS-CoV-2 drugs. [ABSTRACT FROM AUTHOR]

Published
2024
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86. Reconstitution of RNA cap methylation reveals different features of SARS‐CoV‐2 and SARS‐CoV methyltransferases.

Author

He, Miao, Cao, Liu, Liu, Lihong, Jin, Xu, Zheng, Birong, Liu, Xue, Zhuang, Jiaxin, Zhang, Fushi, Yang, Zixiao, Ji, Yanxi, Xu, Tiefeng, Huang, Siyao, Chen, Junhai, Xie, Luyang, Li, Kun, Hou, Panpan, Pan, Jian, Guo, Deyin, and Li, Chunmei

Abstract

Cap RNA methylations play important roles in the replication, evasion of host RNA sensor recognition, and pathogenesis. Coronaviruses possess both guanine N7‐ and 2′‐O‐ribose methyltransferases (N7‐MTase and 2′‐O‐MTase) encoded by nonstructural protein (nsp) 14 and nsp16/10 complex, respectively. In this study, we reconstituted the two‐step RNA methylations of N7‐MTase and 2′‐O‐MTase of severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) in vitro and demonstrated its common and different features in comparison with that of SARS‐CoV. We revealed that the nsp16/10 2′‐O‐MTase of SARS‐CoV‐2 has a broader substrate selectivity than the counterpart of SARS‐CoV and can accommodate both unmethylated and uncapped RNA substrates in a sequence‐independent manner. Most intriguingly, the substrate selectivity of nsp16/10 complex is not determined by the apoenzyme of nsp16 MTase but by its cofactor nsp10. These results provide insight into the unique features of SARS‐CoV‐2 MTases and may help develop strategies to precisely intervene in the methylation pathway and pathogenesis of SARS‐CoV‐2. [ABSTRACT FROM AUTHOR]

Published
2024
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