186020-77-9

Upstream product

• 112-27-6 2,2'-[1,2-ethanediylbis(oxy)]bisethanol 
• 186020-70-2 (E)-17-[N-(9-fluorenylmethoxycarbonyl)-L-alanyloxy]-4,7,10,13-tetraoxa-15-heptadecenoic acid tert-butyl ester 
• 186020-66-6 3-{2-[2-(2-hydroxy-ethoxy)-ethoxy]-ethoxy}-propionic acid tert-butyl ester 
• 166668-33-3 (E)-17-bromo-4,7,10,13-tetraoxa-15-heptadecenoic acid tert-butyl ester 
• 196097-59-3 (E)-17-[N-(9-fluorenylmethoxycarbonyl)-L-alanyloxy]-4,7,10,13-tetraoxa-15-heptadecenoic acid 

Relevant academic research and scientific papers

HYCRON, an Allylic Anchor for High-Efficiency Solid Phase Synthesis of Protected Peptides and Glycopeptides

The recently developed allylic HYCRON anchor1 exhibits excellent properties for the solid phase synthesis of protected peptides and glycopeptides. Model reactions with analogous low molecular weight compounds assessed the acid- and base-stability of the polar and flexible HYCRON linkage. The new anchor is available in a two-step synthesis and allows the use of both the Boc- and the Fmoc-strategy, which can even be combined within one synthesis. Protected glycopeptides are released under almost neutral conditions, taking advantage of the Pd(0)-catalyzed allyl transfer to a weakly basic nucleophile such as N-methylaniline. The highly efficient synthesis of O-αGalNAc-(TN)-peptides of the MUC-1 repeating unit is described. Acid- and base-stability of the allyl ester linkage enabled the synthesis of an O-glucosylated peptide by first removing a threonine tert-butyl group on the solid phase and subsequently glycosylating the liberated resin-bound hydroxyl component.