172348-61-7

Basic information

• Product Name: (1-benzyl-2-{2-[4-(tert-butoxycarbonylamino-methyl)-benzylcarbamoyl]-pyrrolidin-1-yl}-2-oxo-ethyl)-carbamic acid tert-butyl ester
• Synonyms: (1-benzyl-2-{2-[4-(tert-butoxycarbonylamino-methyl)-benzylcarbamoyl]-pyrrolidin-1-yl}-2-oxo-ethyl)-carbamic acid tert-butyl ester
• CAS NO: 172348-61-7
• Molecular Weight: 580.725
• Mol File: 172348-61-7.mol
• Article Data: 2

Chemical Properties

• CAS DataBase Reference: (1-benzyl-2-{2-[4-(tert-butoxycarbonylamino-methyl)-benzylcarbamoyl]-pyrrolidin-1-yl}-2-oxo-ethyl)-carbamic acid tert-butyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: (1-benzyl-2-{2-[4-(tert-butoxycarbonylamino-methyl)-benzylcarbamoyl]-pyrrolidin-1-yl}-2-oxo-ethyl)-carbamic acid tert-butyl ester(172348-61-7)
• EPA Substance Registry System: (1-benzyl-2-{2-[4-(tert-butoxycarbonylamino-methyl)-benzylcarbamoyl]-pyrrolidin-1-yl}-2-oxo-ethyl)-carbamic acid tert-butyl ester(172348-61-7)

Safety Data

• Hazardous Substances Data: 172348-61-7(Hazardous Substances Data)

Upstream product

• 41324-66-7 H-Pro-OBzl 
• 64471-88-1 (S)-benzyl 1-((R)-2-(tert-butoxycarbonylamino)-3-phenylpropanoyl)pyrrolidine-2-carboxylate 
• 18942-49-9 Boc-D-Phe-OH 
• 38675-10-4 N-[(1,1-dimethylethoxy)carbonyl]-D-phenylalanyl-L-proline 
• 108468-00-4 tert-butyl 4-(aminomethyl)benzylcarbamate 

Downstream Products

• 787525-83-1 (S)-1-((R)-2-Amino-3-phenyl-propionyl)-pyrrolidine-2-carboxylic acid 4-aminomethyl-benzylamide 

Relevant articles and documents

How a Fragment Draws Attention to Selectivity Discriminating Features between the Related Proteases Trypsin and Thrombin

In the S1 pocket, the serine proteases thrombin and trypsin commonly feature Asp189 and a Ala190Ser and Glu192Gln exchange. Nevertheless, thrombin cleaves peptide chains solely after Arg, and trypsin after Lys and Arg. Thrombin exhibits a Na+-binding site next to Asp189, which is missing in trypsin. The fragment benzylamine shows direct H-bonding to Asp189 in trypsin, while in thrombin, it forms an H-bond to Glu192. A series of fragments and expanded ligands were studied against both enzymes and mutated variants by crystallography and ITC. The selectivity-determining features of both S1 pockets are difficult to assign to one dominating factor. The Ala190Ser and Glu192Gln replacements may be regarded as highly conserved as no structural and affinity changes are observed between both proteases. With respect to charge distribution, Glu192, together with the thrombin-specific sodium ion, helps in creating an electrostatic gradient across the S1 pocket. This feature is definitely absent in trypsin but important for selectivity along with solvation-pattern differences in the S1 pocket.