1219136-27-2

Upstream product

• 24424-99-5 di-tert-butyl dicarbonate 
• 51-35-4 4R-4-hydroxyproline 
• 13726-69-7 (2S,4R)-4-hydroxy-1-[(2-methylpropan-2-yl)oxycarbonyl]pyrrolidine-2-carboxylic acid 
• 89813-47-8 N-(tert-butoxycarbonyl)-(2S,4R)-4-hydroxyproline benzyl ester 

Downstream Products

• 1219136-30-7 (2S,4R)-2-benzyl 1-tert-butyl 4-((R)-2-amino-3-ethoxy-3-oxopropylsulfanyl)pyrrolidine-1,2-dicarboxylate 
• 178267-93-1 (5S,9R,12S,15S,17aS)-5,15-Diethyl-12-hydroxymethyl-9-phenyl-3,5,6,9,10,12,13,15,16,17a-decahydro-8H-3a,6,10,13,16-pentaaza-cyclopentacyclohexadecene-4,7,11,14,17-pentaone 
• 865469-49-4 (S)-2-benzyl 1-tert-butyl 1H-pyrrole-1,2(2H,5H)-dicarboxylate 
• 565185-32-2 N-Boc-4,5-dehydroproline benzyl ester 
• 865469-50-7 N-(tert-Butoxycarbonyl)-(2S,3R,4S)-3,4-dihydroxyproline benzyl ester 

Relevant academic research and scientific papers

Design and synthesis of plant cyclopeptide Astin C analogues and investigation of their immunosuppressive activity

To further investigate on the structure-activity relationships of immunosuppressive Astin C, seventeen analogues 1–17 were designed and synthetized via amino acid substitution strategy by the solid-phase peptide synthesis method for the first time. In comparison with Astin C (IC50 = 12.6 ± 3.3 μM), only compounds 2 (IC50 = 38.4 ± 16.2 μM), 4 (IC50 = 51.8 ± 12.7 μM), 5 (IC50 = 65.2 ± 15.6 μM), and 8 (IC50 = 61.8 ± 12.4 μM) exhibited immunosuppressive activity in the Lymph node cells of mice. These results showed that the Astin C analogues containing D-amino acid residues, hydrophobic long-chain alkyl substituents, and aryl substituents performed better than those carrying hydrophilic amino acid residues and short-chain alkyl substituents. Moreover compounds 15, 16, and 17 had no immunosuppressive activity, which suggested that cis-3,4-dichlorinated proline played an important role in the immunosuppressive activity of Astin C.

Novel sulfur and selenium containing bis-α-amino acids from 4-hydroxyproline

The synthesis of new substituted prolines carrying at C-4 a second α-amino acid residue is reported. The amino acid, l-cysteine or l-selenocysteine, is linked to the proline ring through the sulfur or the selenium atom, respectively. The products were prepared with different stereochemistry at C-4, in few and clean high-yielding steps, with suitable protections for solid phase applications. The introduction of both sulfur and selenium atoms at C-4 of the proline ring seems to enhance significantly the cis geometry at the prolyl amide bond.