1056288-48-2

Upstream product

• 139109-03-8 (Z)-1-[(tert-butyldiphenylsilyl)oxy]-3,7-dimethyl-2,6-octadiene 
• 58479-61-1 tert-butylchlorodiphenylsilane 
• 201670-51-1 (Z)-1-(tert-butyldiphenylsilyloxy)-6,7-epoxy-3,7-dimethylocta-2-ene 
• 201670-50-0 (Z)-3-Bromo-8-(tert-butyl-diphenyl-silanyloxy)-2,6-dimethyl-oct-6-en-2-ol 
• 139109-04-9 (Z)-1-[(tert-butyldiphenylsilyl)oxy]-3-methyl-2-hexen-6-al 
• 106-25-2 Nerol 
• 201670-54-4 (2Z,6Z)-1-O-(tert-butyldiphenylsilyl)-3,7-dimethylocta-2,6-dien-1,8-diol 
• 1528749-24-7 C₄₁H₄₆OPSi⁽¹⁺⁾*I^(1-) 
• 1528749-23-6 (Z)-1-O-tert-butyldiphenylsilyl-3-methyl-6-O-(4-toluenesulfonyl)hexa-2-en-1,6-diol 
• 1528749-25-8 (2Z,6Z)-1-(tert-butyldiphenylsilyloxy)-3,7-dimethyl-8-(2-tetrahydropyranyloxy)octa-2,6-diene 
• 1528749-22-5 (Z)-1-O-tert-butyldiphenylsilyl-3-methyl-6-O-(4-toluenesulfonyl)hexa-2-en-1,6-diol 
• 930803-78-4 (Z)-1-O-tert-butyldiphenylsilyl-3-methylhexa-2-en-1,6-diol 

Downstream Products

• 1056289-79-2 (2Z,6Z,10Z,14Z)-9-(benzenesulfonyl)-1-(tert-butyldiphenylsilyloxy)-16-chloro-3,7,11,15-tetramethylhexadeca-2,6,10,14-tetraene 
• 1218987-81-5 C₄₇H₆₄O₅SSi 
• 68982-81-0 (2Z,6Z,10Z)-3,7,11,15-tetramethylhexadeca-2,6,10,14-tetraen-1-yl phosphate 
• 1056288-54-0 C₄₇H₆₄O₃SSi 

Relevant academic research and scientific papers

N-GLYCOSYLATION OF PEPTIDES AND PROTEINS

A process for the production of a glycoconjugate by N-glycosylation of a protein or peptide comprising the sequence D/E-X-N-X-S/T, wherein each X is the same or different and is any natural amino acid other than proline, wherein the process comprises reacting the protein or peptide with a polyisoprenyl pyrophosphate of formula (I), or a salt thereof, in the presence of PglB: (I) to produce the glycoconjugate comprising the protein or peptide having a saccharide [SI] linked to the asparagine in the sequence D/E-X-N-X-S/T. Polyisoprenylpyrophosphates used as substrates in the biocatalytic process are also provided, as well as certain glycoconjugates.

Rationally designed short polyisoprenol-linked PglB substrates for engineered polypeptide and protein N-glycosylation

The lipid carrier specificity of the protein N-glycosylation enzyme C. jejuni PglB was tested using a logical, synthetic array of natural and unnatural C10, C20, C30, and C40 polyisoprenol sugar pyrophosphates, including those bearing repeating cis-prenyl units. Unusual, short, synthetically accessible C20 prenols (nerylnerol 1d and geranylnerol 1e) were shown to be effective lipid carriers for PglB sugar substrates. Kinetic analyses for PglB revealed clear KM-only modulation with lipid chain length, thereby implicating successful in vitro application at appropriate concentrations. This was confirmed by optimized, efficient in vitro synthesis allowing >90% of Asn-linked β-N-GlcNAc-ylated peptide and proteins. This reveals a simple, flexible biocatalytic method for glycoconjugate synthesis using PglB N-glycosylation machinery and varied chemically synthesized glycosylation donor precursors.