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Synthesis, biological evaluation, and molecular modeling of berberine derivatives as potent acetylcholinesterase inhibitors.
Bioorg Med Chem. 2010 Feb; 18(3):1244-51.BM

Abstract

By targeting the dual active sites of acetylcholinesterase (AChE), a new series of berberine derivatives was designed, synthesized, and evaluated as AChE inhibitors. Most of the derivatives inhibited AChE in the sub-micromolar range. Compound 8c, berberine linked with phenol by a 4-carbon spacer, showed the most potent inhibition of AChE. A kinetic study of AChE and BuChE indicated that a mix-competitive binding mode existed for these berberine derivatives. Molecular modeling studies confirmed that these hybrids target both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. This is the first report where AChE inhibitory activity has been associated with berberine as a lead molecule.

Authors+Show Affiliations

The Industrial Institute of Fine Chemicals and Synthetic Drugs, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20056426

Citation

Huang, Ling, et al. "Synthesis, Biological Evaluation, and Molecular Modeling of Berberine Derivatives as Potent Acetylcholinesterase Inhibitors." Bioorganic & Medicinal Chemistry, vol. 18, no. 3, 2010, pp. 1244-51.
Huang L, Shi A, He F, et al. Synthesis, biological evaluation, and molecular modeling of berberine derivatives as potent acetylcholinesterase inhibitors. Bioorg Med Chem. 2010;18(3):1244-51.
Huang, L., Shi, A., He, F., & Li, X. (2010). Synthesis, biological evaluation, and molecular modeling of berberine derivatives as potent acetylcholinesterase inhibitors. Bioorganic & Medicinal Chemistry, 18(3), 1244-51. https://doi.org/10.1016/j.bmc.2009.12.035
Huang L, et al. Synthesis, Biological Evaluation, and Molecular Modeling of Berberine Derivatives as Potent Acetylcholinesterase Inhibitors. Bioorg Med Chem. 2010;18(3):1244-51. PubMed PMID: 20056426.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Synthesis, biological evaluation, and molecular modeling of berberine derivatives as potent acetylcholinesterase inhibitors. AU - Huang,Ling, AU - Shi,Anding, AU - He,Feng, AU - Li,Xingshu, Y1 - 2009/12/16/ PY - 2009/10/22/received PY - 2009/12/09/revised PY - 2009/12/10/accepted PY - 2010/1/9/entrez PY - 2010/1/9/pubmed PY - 2010/5/14/medline SP - 1244 EP - 51 JF - Bioorganic & medicinal chemistry JO - Bioorg Med Chem VL - 18 IS - 3 N2 - By targeting the dual active sites of acetylcholinesterase (AChE), a new series of berberine derivatives was designed, synthesized, and evaluated as AChE inhibitors. Most of the derivatives inhibited AChE in the sub-micromolar range. Compound 8c, berberine linked with phenol by a 4-carbon spacer, showed the most potent inhibition of AChE. A kinetic study of AChE and BuChE indicated that a mix-competitive binding mode existed for these berberine derivatives. Molecular modeling studies confirmed that these hybrids target both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. This is the first report where AChE inhibitory activity has been associated with berberine as a lead molecule. SN - 1464-3391 UR - https://www.unboundmedicine.com/medline/citation/20056426/Synthesis_biological_evaluation_and_molecular_modeling_of_berberine_derivatives_as_potent_acetylcholinesterase_inhibitors_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0968-0896(09)01127-4 DB - PRIME DP - Unbound Medicine ER -