{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lin X"],"funding":["Drug safety research project of Guangxi Zhuang Autonomous Region Drug Administration","Guangxi Natural Science Foundation","2022 Guangxi Higher Education Institutions Young and Middle-aged Teachers Scientific Research Basic Ability Enhancement Project","National Natural Science Foundation of China","Self-financed scientific research of Guangxi Zhuang Autonomous Region Health Commission in 2022","Self-financed scientific research of Guangxi Zhuang Autonomous Region Health Commission"],"pagination":["1961"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11085145"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["29(9)"],"pubmed_abstract":["In this study, two \"on-off\" probes (BF<sub>2</sub>-cur-Ben and BF<sub>2</sub>-cur-But) recognizing acetylcholinesterase (AChE) were designed and synthesized. The obtained probes can achieve recognition of AChE with good selectivity and pH-independence with a linear range of 0.5~7 U/mL and 0.5~25 U/mL respectively. BF<sub>2</sub>-cur-Ben has a lower limit of detection (LOD) (0.031 U/mL), higher enzyme affinity (K<sub>m</sub> = 16 ± 1.6 μM), and higher inhibitor sensitivity. A responsive mechanism of the probes for AChE was proposed based on HPLC and mass spectra (MS) experiments, as well as calculations. In molecular simulation, BF<sub>2</sub>-cur-Ben forms more hydrogen bonds (seven, while BF<sub>2</sub>-cur-But has only four) and thus has a more stable enzyme affinity, which is mirrored b"],"journal":["Molecules (Basel, Switzerland)"],"pubmed_title":["Two Fluorescent Probes for Recognition of Acetylcholinesterase: Design, Synthesis, and Comparative Evaluation."],"pmcid":["PMC11085145"],"funding_grant_id":["GYJK (2023)003","2022GXNSFAA035453","Z-A20221011","22267002","2022KY1387"],"pubmed_authors":["Qing B","Jiang J","Zou L","Jiang F","Huang J","Lin X","Liu Q","Yi Q","Lan W","Wang J","Wang M","Lai Z","Huang X"],"additional_accession":[]},"is_claimable":false,"name":"Two Fluorescent Probes for Recognition of Acetylcholinesterase: Design, Synthesis, and Comparative Evaluation.","description":"In this study, two \"on-off\" probes (BF<sub>2</sub>-cur-Ben and BF<sub>2</sub>-cur-But) recognizing acetylcholinesterase (AChE) were designed and synthesized. The obtained probes can achieve recognition of AChE with good selectivity and pH-independence with a linear range of 0.5~7 U/mL and 0.5~25 U/mL respectively. BF<sub>2</sub>-cur-Ben has a lower limit of detection (LOD) (0.031 U/mL), higher enzyme affinity (K<sub>m</sub> = 16 ± 1.6 μM), and higher inhibitor sensitivity. A responsive mechanism of the probes for AChE was proposed based on HPLC and mass spectra (MS) experiments, as well as calculations. In molecular simulation, BF<sub>2</sub>-cur-Ben forms more hydrogen bonds (seven, while BF<sub>2</sub>-cur-But has only four) and thus has a more stable enzyme affinity, which is mirrored b","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-04-24T03:16:00.677Z","creation":"2026-04-24T03:10:05.581Z"},"accession":"S-EPMC11085145","cross_references":{"pubmed":["38731452"],"doi":["10.3390/molecules29091961"]}}