Synthesis of isobutyl-C-galactoside (IBCG) as an isopropylthiogalactoside (IPTG) substitute for increased induction of protein expression.
[reaction: see text] Addition of isopropyl-beta-d-thiogalactopyranoside (IPTG) to bacterial cultures is often used to induce expression of plasmid-based genes for the production of recombinant proteins under control of the lac promoter, but a simple method to circumvent the inherent instability of this compound has not been addressed experimentally. Herein we report the first synthesis of isobutyl-C-galactoside (IBCG), the C-glycoside analogue of IPTG, and show that IBCG is superior to IPTG in inducing protein expression over long induction times.
Ko
Kwang-Seuk
KS
Department of Chemistry and the Plant Sciences Institute, Gilman Hall, Iowa State University, Ames, Iowa 50011-3111, USA.
Kruse
Jerrid
J
Pohl
Nicola L
NL
D004247:DNA / Q000096:biosynthesis / Q000235:genetics; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics* / Q000378:metabolism; D005697:Galactosides / Q000494:pharmacology*; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects*; D049452:Green Fluorescent Proteins; D007544:Isopropyl Thiogalactoside / Q000138:chemical synthesis*; D007763:Lac Operon / Q000235:genetics; D008164:Luminescent Proteins; D014176:Protein Biosynthesis
D005697:Galactosides; D008164:Luminescent Proteins; C476523:isobutyl-C-galactoside; D049452:Green Fluorescent Proteins; D007544:Isopropyl Thiogalactoside; D004247:DNA