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.
Department of Chemistry and the Plant Sciences Institute, Gilman Hall, Iowa State University, Ames, Iowa 50011-3111, USA.
Kwang-Seuk
KS
Ko
Jerrid
J
Kruse
Nicola L
NL
Pohl
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