188292-89-9

Upstream product

• 35793-73-8 N-(tert-butyloxycarbonyl)-γ-benzyl-D-glutamic acid 
• 63091-98-5 benzyl N²-(tert-butoxycarbonyl)-N¹-methyl-D-glutaminate 

Downstream Products

• 190586-75-5 N-tert-butoxycarbonyl-L-seryl-D-glutamic acid 1-methylamide 5-benzyl ester 
• 211678-13-6 -D-glutamic acid 1-methylamide 5-benzyl ester 
• 190587-52-1 (R)-4-Methylcarbamoyl-4-[(R)-2-(2-tetradecyl-hexadecanoylamino)-3-((2R,3S,4R,5R,6S)-3,4,5-tris-benzyloxy-6-methyl-tetrahydro-pyran-2-yloxy)-propionylamino]-butyric acid benzyl ester 
• 190587-48-5 (R)-4-Methylcarbamoyl-4-[(S)-2-(2-tetradecyl-hexadecanoylamino)-3-((2R,3S,4R,5R,6S)-3,4,5-tris-benzyloxy-6-methyl-tetrahydro-pyran-2-yloxy)-propionylamino]-butyric acid benzyl ester 
• 190587-45-2 N-(tert-butoxycarbonyl)-O-(2,3,4-tri-O-benzyl-α-L-fucopyranosyl)-D-seryl-D-glutamic acid 1-methylamide 5-benzyl ester 
• 190587-43-0 N-(tert-butoxycarbonyl)-O-(2,3,4-tri-O-benzyl-α-L-fucopyranosyl)-L-seryl-D-glutamic acid 1-methylamide 5-benzyl ester 
• 190587-53-2 (R)-4-[(R)-2-Amino-3-((2R,3S,4R,5R,6S)-3,4,5-tris-benzyloxy-6-methyl-tetrahydro-pyran-2-yloxy)-propionylamino]-4-methylcarbamoyl-butyric acid benzyl ester 
• 190587-49-6 (R)-4-[(S)-2-Amino-3-((2R,3S,4R,5R,6S)-3,4,5-tris-benzyloxy-6-methyl-tetrahydro-pyran-2-yloxy)-propionylamino]-4-methylcarbamoyl-butyric acid benzyl ester 
• 190587-18-9 [N-(2-tetradecylhexadecanoyl)-O-(2,3,5-tri-O-benzyl-α-L-fucofuranosyl)-L-seryl]-D-glutamic acid 1-methylamide 5-benzyl ester 
• 190587-00-9 [N-(tert-butoxycarbonyl)-O-(2,3,5-tri-O-benzyl-α-L-fucofuranosyl)-L-seryl]-D-glutamic acid 1-methylamide 5-benzyl ester 
• 190587-19-0 (R)-4-{(S)-2-Amino-3-[(2R,3S,4R,5R)-3,4-bis-benzyloxy-5-((S)-1-benzyloxy-ethyl)-tetrahydro-furan-2-yloxy]-propionylamino}-4-methylcarbamoyl-butyric acid benzyl ester 
• 211678-22-7 -D-glutamic acid 1-methylamide 5-benzyl ester 
• 211678-18-1 -D-glutamic acid 1-methylamide 5-benzyl ester 
• 211678-15-8 -D-glutamic acid 1-methylamide 5-benzyl ester 

Relevant academic research and scientific papers

Studies on selectin blockers. 7. Structure-activity relationships of sialyl Lewis X mimetics based on modified ser-glu dipeptides

We have previously found that heterochiral fucodipeptides, L-Ser-D-Glu (3a) and D-Ser-L-Glu (3b), exhibited up to 20-100 times more potency than a sialyl Lewis X (sLe(X), 1) and a 3'sulfated Lewis X analogue (2) toward E- selectin binding and have also proposed, from molecular dynamics calculation, that their strong activities would depend on a possible formation of the type II and/or type II' β-turn of compounds 3a,b (Tsukida, T.; Hiramatsu, Y.; Tsujishita, H.; Kiyoi, T.; Yoshida, M.; Kurokawa, K.; Moriyama, H.; Ohmoto, H.; Wada, Y.; Saito, T.; Kondo, H. J. Med. Chem. 1997, 40, 3534-3541). To clarify our hypothesis, we synthesized several analogues of compounds 3a,b and investigated their structure-activity relationships. As a result, it was indicated that the type II and/or type II' β-turn conformation would be a comparatively tight form and would play important roles in favorable binding to E-selectin. These findings indicate that sLe(X) mimetics with type II and type II' β-turn dipeptides could be a useful methodology for the design of an active selectin blocker.

Studies on selection blockers. 5. Design, synthesis, and biological profile of sialyl Lewis x mimetics based on modified serine-glutamic acid dipeptides.

We have rationally designed a sLe(x) mimetic based on molecular modeling, synthesized type II and type II' beta-turn dipeptides (3a,b), and evaluated their biological profiles both in vitro and in vivo. Against E-selectin-sLe(x) binding, the type II beta-turn dipeptide L-Ser-D-Glu 3a (IC50, 13 microM) and the type II' beta-turn dipeptide D-Ser-L-Glu 3b (IC50, 5.5 microM) were 20-100-fold more potent blockers than sLe(x) (1; IC50, 600 microM) and a 3'-sulfated Le(x) analog (2; IC50, 280 microM). On the other hand, other stereoisomers, such as L-Ser-L-Glu 3c and D-Ser-D-Glu 3d, were very weak blockers, with IC50 > 1000 microM for both 3c,d. Against the P- and L-selectins, despite much different stereochemistry of compounds 3a-d, the dipeptides 3a-d were all more potent blockers than either sLe(x) or compound 2. Interestingly, compound 3b provided significant in vivo efficacy against an immunoglobulin E-mediated skin reaction in a mouse model. These findings indicate that sLe(x) mimetics with type II and type II' beta-turn dipeptides could be useful in the design of an active selectin blocker in vitro and/or in vivo.