Abstract
This study was funded by the Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior, Brasil (CAPES), Finance Code 001, by the National Council of Scientific and Technological Development (CNPq) and Foundation of Support to Research and Innovation of Espirito Santo (FAPES PPE-Agro No. 76418880/16). We also would like to acknowledge INCTBioNat (CNPq 465637/2014-0) for additional support and NCQP-UFES, as well as the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2019 unit and BioTecNorte operation (NORTE-01-0145-FEDER-000004) funded by the European Regional Development Fund under the scope of Norte2020, Programa Operacional Regional do Norte. L. R. R. also acknowledges her sabbatical leave fellowship (SFRH/BSAB/142991/2018) funded by FCT. D. F. is recipient of a doctoral fellowship (call NORTE-69-2015-15) funded by the European Social Fund under the scope of Norte2020, Programa Operacional Regional do Norte.
Highlights
Isatin (1H-indole-2,3-dione), first synthesized by Erdmann[1] and Laurent[2] in 1840, results from the reaction of indigo with nitric and chromium acids
We describe the synthesis of 11 isatin derivatives that were obtained in low to high yields
Comercial isatin was used as a starting material for bimolecular nucleophilic substitution and a click chemistry approach to develop all described chemical reactions
Summary
Isatin (1H-indole-2,3-dione), first synthesized by Erdmann[1] and Laurent[2] in 1840, results from the reaction of indigo with nitric and chromium acids. Ser[9] and Tyr[28] phosphorylation is a precondition for enzymatic action regulation since these residues control the gate of the substrate-binding site.[30,31] Ser[9] is an auto-inhibition site that inhibits the catalytic activity when phosphorylated This phosphorylation site is disordered in GSK-3β crystals and not identified in crystallographic information. Due to absence of a threonine residue, following phosphorylation of the serine residue, Ser[9], the GSK-3β N-terminal region binds to and blocks the catalytic site.[29,32] there is an important similarity between enzyme and apoenzyme structures, and the GSK‐3β protein crystallographic structure presented as a dimer with identical subunits. The infrared (IR) spectrum was recorded on a Bruker Tensor 27 FT-IR Spectrometer (Bremen, Germany), equipped with a Pike MIRacle attenuated total reflection (ATR) assembly with a ZnSe crystal, scanning from 4000 to 600 cm-1
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