1451369-69-9

Upstream product

• 1451369-66-6 4-methylphenyl 2-O-(2-naphthyl)methyl-3,5-O-(tetraisopropyldisiloxane-1,3-diyl)-1-thio-α-L-arabinofuranoside 
• 13504-85-3 (2S,4R)-1-(benzyloxycarbonyl)-4-hydroxypyrrolidine-2-carboxylic acid 
• 1451369-68-8 N-benzyloxycarbonyl-4R-[3,5-O-(tetraisopropyldisiloxane-1,3-diyl)-β-L-arabinofuranosyl]oxy-L-proline benzyl ester 
• 939-26-4 2-bromomethylnaphthyl bromide 

Relevant academic research and scientific papers

Synthesis of the highly glycosylated hydrophilic motif of extensins

Extensin, the structural motif of plant extracellular matrix proteins, possesses a unique highly glycosylated, hydrophilic, and repeating Ser 1Hyp4 pentapeptide unit, and has been proposed to include post-translational hydroxylation at proline residue and subsequent oligo-L-arabinosylations at all of the resultant hydroxyprolines as well as galactosylation at serine residue. Reported herein is the stereoselective synthesis of one of the highly glycosylated motifs, Ser(Galp1)- Hyp(Araf4)-Hyp(Araf4)-Hyp(Araf3)-Hyp(Araf 1). The synthesis has been completed by the application of 2-(naphthyl)methylether-mediated intramolecular aglycon delivery to the stereoselective construction of the Ser(Galp1) and Hyp(Araf n) fragments as the key step, as well as Fmoc solid-phase peptide synthesis for the backbone pentapeptide.

Stereoselective synthesis of Arabidopsis CLAVATA3 (CLV3) glycopeptide, unique protein post-translational modifications of secreted peptide hormone in plant

The unique hydroxylproline (Hyp)-linked O-glycan modification is a common process in hydroxyproline-rich glycoproteins (HRGPs). The modification occurs through post-translational hydroxylation at 4-position of proline residues some of which are followed by O-glycosylation at the resulting Hyp which is also found in some secreted peptide hormones such as CLAVATA3 (CLV3) of Arabidopsis thaliana plants. An active mature CLV3 is a tridecapeptide linked to β-l-Araf-(1→2)-β-l-Araf-(1→2)-β-l-Araf at a Hyp residue in the center of the peptide sequence such as Arg-Thr-Val-Hyp-Ser-Gly-Hyp(l- Arafn)-Asp-Pro-Leu-His-His-His (n = 3). We report here the synthesis of the secreted and modified CLV3 glycopeptide with all glycoforms (Araf 0-3CLV3) of A. thaliana plants. A highly stereoselective β-arabinofuranosylation of Hyp derivatives as the key step of the synthesis of CLV3 glycopeptide was achieved by NAP ether-mediated IAD, which was effectively applied to the synthesis of oligoarabinosylated hydroxylproline [Hyp(l-Araf1-3)] derivatives. Fmoc-solid phase peptide synthesis was carried out using COMU as the coupling reagent for the introduction of [Hyp(l-Araf0-3)] derivatives as well as further elongation to the CLV3 glycopeptides.