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Chemical synthesis, in vitro acetohydroxyacid synthase (AHAS) inhibition, herbicidal activity, and computational studies of isatin derivatives.
J Agric Food Chem. 2011 Sep 28; 59(18):9892-900.JA

Abstract

Acetohydroxyacid synthase (AHAS) catalyzes the first common step in the biosynthesis of the branched-chain amino acids. As a result of its metabolic importance in plants, it is a target for many commercial herbicides. Virtual screening analysis inspired the evaluation of 19 commercially available isatin analogues and 13 newly synthesized isatin derivatives as novel AHAS inhibitors and for their herbicidal activity. The best compound demonstrated 95% inhibition of the activity of Arabidopsis thaliana AHAS at a concentration of 100 mg L(-1), whereas the herbicidal activities of three compounds reached 50% inhibition at a concentration of 10 mg L(-1) using the rape root growth test. CoMFA contour models were established to understand the structure-activity relationships for this class of AHAS inhibitor. The compounds were docked to the active site cavity of A. thaliana AHAS using FlexX, and the dominant binding mode was consistent with frontier molecular orbital from DFT calculations. This is the first comprehensive study of isatin derivatives as AHAS inhibitors and provides a valuable starting point for the design of new herbicides.

Authors+Show Affiliations

State-Key Laboratory and Institute of Elemento-Organic Chemistry, Nankai University, Tianjin 300071, China. nkwjg@nankai.edu.cnNo affiliation info availableNo affiliation info availableNo 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

21838297

Citation

Wang, Jianguo, et al. "Chemical Synthesis, in Vitro Acetohydroxyacid Synthase (AHAS) Inhibition, Herbicidal Activity, and Computational Studies of Isatin Derivatives." Journal of Agricultural and Food Chemistry, vol. 59, no. 18, 2011, pp. 9892-900.
Wang J, Tan H, Li Y, et al. Chemical synthesis, in vitro acetohydroxyacid synthase (AHAS) inhibition, herbicidal activity, and computational studies of isatin derivatives. J Agric Food Chem. 2011;59(18):9892-900.
Wang, J., Tan, H., Li, Y., Ma, Y., Li, Z., & Guddat, L. W. (2011). Chemical synthesis, in vitro acetohydroxyacid synthase (AHAS) inhibition, herbicidal activity, and computational studies of isatin derivatives. Journal of Agricultural and Food Chemistry, 59(18), 9892-900. https://doi.org/10.1021/jf2021607
Wang J, et al. Chemical Synthesis, in Vitro Acetohydroxyacid Synthase (AHAS) Inhibition, Herbicidal Activity, and Computational Studies of Isatin Derivatives. J Agric Food Chem. 2011 Sep 28;59(18):9892-900. PubMed PMID: 21838297.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Chemical synthesis, in vitro acetohydroxyacid synthase (AHAS) inhibition, herbicidal activity, and computational studies of isatin derivatives. AU - Wang,Jianguo, AU - Tan,Haizhong, AU - Li,Yonghong, AU - Ma,Yi, AU - Li,Zhengming, AU - Guddat,Luke W, Y1 - 2011/08/25/ PY - 2011/8/16/entrez PY - 2011/8/16/pubmed PY - 2012/1/14/medline SP - 9892 EP - 900 JF - Journal of agricultural and food chemistry JO - J. Agric. Food Chem. VL - 59 IS - 18 N2 - Acetohydroxyacid synthase (AHAS) catalyzes the first common step in the biosynthesis of the branched-chain amino acids. As a result of its metabolic importance in plants, it is a target for many commercial herbicides. Virtual screening analysis inspired the evaluation of 19 commercially available isatin analogues and 13 newly synthesized isatin derivatives as novel AHAS inhibitors and for their herbicidal activity. The best compound demonstrated 95% inhibition of the activity of Arabidopsis thaliana AHAS at a concentration of 100 mg L(-1), whereas the herbicidal activities of three compounds reached 50% inhibition at a concentration of 10 mg L(-1) using the rape root growth test. CoMFA contour models were established to understand the structure-activity relationships for this class of AHAS inhibitor. The compounds were docked to the active site cavity of A. thaliana AHAS using FlexX, and the dominant binding mode was consistent with frontier molecular orbital from DFT calculations. This is the first comprehensive study of isatin derivatives as AHAS inhibitors and provides a valuable starting point for the design of new herbicides. SN - 1520-5118 UR - https://www.unboundmedicine.com/medline/citation/21838297/Chemical_synthesis_in_vitro_acetohydroxyacid_synthase__AHAS__inhibition_herbicidal_activity_and_computational_studies_of_isatin_derivatives_ L2 - https://dx.doi.org/10.1021/jf2021607 DB - PRIME DP - Unbound Medicine ER -