178488-33-0

Upstream product

• 51-35-4 4R-4-hydroxyproline 
• 130930-25-5 (R,R)-4-hydroxy-1-(benzyloxycarbonyl)pyrrolidine-2-carboxylic acid 
• 2584-71-6 cis-hydroxy-D-proline 
• 114676-59-4 (2R,4R)-4-hydroxy-2-methoxycarbonylpyrrolidine hydrochloride 
• 501-53-1 benzyl chloroformate 
• 124-63-0 methanesulfonyl chloride 
• 155075-23-3 (2R,4R)-1-benzyl 2-methyl 4-hydroxypyrrolidine-1,2-dicarboxylate 

Downstream Products

• 153076-64-3 (R)-2,5-Dihydro-pyrrole-1,2-dicarboxylic acid 1-benzyl ester 2-ethyl ester 
• 178271-98-2 (2R,3S,4R)-3,4-Dihydroxy-pyrrolidine-1,2-dicarboxylic acid 1-benzyl ester 
• 178272-08-7 (2R,3S,4R)-3,4-Dihydroxy-pyrrolidine-1,2-dicarboxylic acid 1-benzyl ester 2-ethyl ester 
• 178271-96-0 (2R,3S,4R)-2-[(1S,2R)-1-Ethoxycarbonyl-2-((2R,3S,4R,5R,6S)-3,4,5-tris-benzyloxy-6-methyl-tetrahydro-pyran-2-yloxy)-propylcarbamoyl]-3,4-dihydroxy-pyrrolidine-1-carboxylic acid benzyl ester 
• 178271-97-1 5-{(2R,3S,4R)-2-[(1S,2R)-1-Ethoxycarbonyl-2-((2R,3S,4R,5R,6S)-3,4,5-tris-benzyloxy-6-methyl-tetrahydro-pyran-2-yloxy)-propylcarbamoyl]-3,4-dihydroxy-pyrrolidin-1-yl}-5-oxo-pentanoic acid benzyl ester 
• 739360-84-0 (2R,4S)-1-benzyl 2-methyl 4-aminopyrrolidine-1,2-dicarboxylate 
• 1253790-74-7 4S-N⁴(t-Boc)-N₁(Fmoc)-D-amino proline 
• 1279034-78-4 (2R,4S)-4-[(tert-butoxycarbonyl)amino]pyrrolidine-2-carboxylic acid 

Relevant academic research and scientific papers

Spiegelmeric 4R/S-hydroxy/amino-L/D-prolyl collagen peptides: conformation and morphology of self-assembled structures

The primary structure of collagen, the major protein in connective tissue of mammals, comprises of repeating triads [(LPro-LHyp-Gly)n, P1, LHyp being 4R-hydroxy-lProline)] in a single strand that adopts left-handed polyproline II type helix. Three such single stranded helices wind around each another and held together by interchain H-bonds to form right-handed triple helix. This manuscript reports on collagen derived from its mirror image triad [(DPro-DHyp-Gly)n, P2, DHyp being 4S-hydroxy-DProline) and its 4-amino analogue (DPro-DAmp-Gly)n P4, DAmp being 4S-amino-DProline that form corresponding spiegelmeric triplexes. The amino L-collagen peptide (LPro-LAmp-Gly)n P3 and its D-analogue P4 show higher thermal stabilities compared to 4-hydroxy-lProline collagen peptides P1 and P2. The enantiomeric peptide pairs show mirror image CD profiles and identical thermal stability, with ionizable 4-amino group in P3 and P4 imparting pH dependent triplex stability. Upon cold mixing of the L- and D-collagen peptides, different morphological nanostructures arise from inter triplex peptide association. When the peptides are hot mixed (annealed), the inter peptide association occurs via interaction of single stranded peptide chains of opposite handedness leading to networked gel formation in P1 and P2, while the charged peptides P3 and P4 show more ordered nanofibers, different from the enantiomerically pure peptides. The nanocomposites of such chiral hybrid peptides may have not only interesting physicomorphology, but also biological properties that need exploration.

Synthesis of sialyl Lewis X mimetics and related structures using the glycosyl phosphite methodology and evaluation of E-selectin inhibition

This paper describes our recent study of glycosyl phosphites for glycosylation reactions, with particular emphasis on the investigation of protecting group and stereochemistry effects on the anomeric reactivity and stereoselectivity, and the application of this methodology to the synthesis of Lewis X (Le(x)), Lewis Y (Le(y)), glycopeptides, and sialyl Lewis X (SLe(x)) mimetics. Both α-O-fucosyl-L-threonine and α-O-fucosyl-(1R,2R)-2-aminocyclohexanol were found to be effective templates for the chemical/enzymatic synthesis of SLe(x) mimetics, and some fucopeptides prepared were 5-10 times more active than SLe(x) as inhibitors of E-selectin.