6491-59-4

Upstream product

• 6913-23-1 2-thioxo-thiazolidin-5-one 
• 516-06-3 D,L-valine 
• 4090-17-9 racemic N-chloroacetylvaline 
• 1160-23-2 N-(N,N-phthaloyl-glycyl)-DL-valine 
• 41089-56-9 Anthranilyl-glyvalin 
• 56-40-6 glycine 
• 118864-66-7 N-glycyl-DL-valine ethyl ester; hydrochloride 
• 118864-66-7 N-glycyl-D-valine ethyl ester; hydrochloride 
• 118864-66-7 glycine-L-leucine ethyl ester hydrochloride 
• 2185-00-4 1,3-oxazolidine-2,5-dione 
• 72-18-4 L-valine 
• 23937-14-6 N-Benzyloxycarbonyl-glycyl-L-valin-<4>picolylester 
• 21760-98-5 L-valine benzyl ester 
• 1138-80-3 N-(Benzyloxycarbonyl)glycine 

Downstream Products

• 16944-60-8 3-isopropyl-piperazine-2,5-dione 
• 10277-41-5 N-(N-phenylacetyl-glycyl)-valine 
• 122411-93-2 N-benzyloxycarbonyl-phenylalanyl=>glycyl=>valine ethyl ester; N-benzyloxycarbonyl-D-phenylalanyl=>glycyl=>D-valine ethyl ester 
• 16944-60-8 (2S)-isopropylpiperazine-3,6-dione 

Relevant academic research and scientific papers

Thermodynamic characteristics of protolytic equilibria in aqueous solutions of glycyl peptides

Protolytic equilibria in aqueous solutions of glycyl-DL-serine, glycyl-DL-threonine, and glycyl-DL-valine are investigated by means of potentiometry and calorimetry. Dissociation constants and heat effects of the above dipeptides are determined. Standard

Rapid, effective deprotection of tert-butoxycarbonyl (Boc) amino acids and peptides at high temperatures using a thermally stable ionic liquid

A method for high temperature Boc deprotection of amino acids and peptides in a phosphonium ionic liquid is described. The ionic liquid had low viscosity, high thermal stability and demonstrated a beneficial effect. The study extended the possibility for extraction of water soluble polar organic molecules using ionic liquids. Trace water significantly improved product purity and yield, while only 2 equiv. TFA led to deprotection within 10 min. The trityl group was also deprotected.

Synthesis of dendritic oligo(aryl sulfone)s as supports for synthesis

A short, divergent route to G1 oligo(aryl sulfone)s and a G 2 oligo(aryl sulfone) dendrimer using nucleophilic aromatic substitution reactions is described. A range of tetrasubstituted pentasulfones are proposed for applications as homogeneous supports for synthesis. Key to achieving selectivity in the syntheses is the activation of leaving groups by sulfide to sulfone oxidation. Preparation of the G2 oligo(aryl sulfone) is low-yielding due to competition from SET processes that are interesting from a mechanistic point of view. The utility of the supports is exemplified with a four step synthesis of a dipeptide and by 'react and release' synthesis of amides.

Cancerous metastasis inhibitor

A chimeric protein wherein HI-8 which is the C-terminal domain of human urinary trypsin inhibitor (UTI) having a cancer cell metastasis inhibitory effect, is linked to a peptide containing the G domain of urokinase binding specifically to urokinase receptor expressed in a large amount in cancer cells.

The pH-rate profile for the hydrolysis of a peptide bond

The rate of hydrolysis of N-(phenylacetyl)glycyl-D-valine (PAGV), an acyclic penicillin G analogue, at pH 0, 1, 3, 5, 7, 9, 11, 13, and 14 has been measured at 37 °C and a pH-rate profile constructed. At each pH, hydrolysis of both the (phenylacetyl)glycyl amide bond and glycyl-D-valine peptide bond was monitored. At pH 3, 5, 7, 9, and 11, the hydrolysis products glycyl-D-valine and D-valine were derivatized with naphthalene-2,3-dialdehyde in the presence of cyanide; the resultant 1-cyano-2-substituted- benz[f]isoindole (CBI) derivatives, which are highly fluorescent, were then quantified using reverse-phase HPLC. The hydrolysis reactions were explicitly shown to be first-order peptide concentration at pH 5 and 9, and all rates were shown to be independent of the buffer concentration. The rates at pH 0, 1, 13, and 14 were measured in 1 M DCl, 0.1 M DCl, 0.1 M NaOD, and 1 M NaOD, respectively, and the hydrolysis products were detected by 1H NMR. The first-order rate constants obtained from the above reactions were fit to the general equation k = k(H2O) + k(H)3(O) [H3O+] + k(OH)-[OH-] to yield the following results: for hydrolysis of the (phenylacetyl)glycyl bond, k(H2O) = (9.05 ± 6.36) x 10-11 s-1, k(H3O)+ = (1.60 ± 1.04) x 10-6 M-1 s-1, and k(OH)- = (1.11 ± 0.73) x 10-6 M-1 s-1; and for hydrolysis of the glycyl-D-valine bond, k(H2O) = (8.23 ± 4.33) x 10-11 s-1, k(H3O)+ = (1.67 ± 0.80) x 10-6 M-1 s-1, and k(OH)- = (1.16 ± 0.56) x 10-6 M-1 s-1. At pH 7, the hydrolysis of both the (phenylacetyl)glycyl amide bond and glycyl-D-valine peptide bond is dominated by k(H2O). The corresponding half-life for (phenylacetyl)glycyl bond hydrolysis is 243 years (with a range of 143-817 years within experimental error), while that for glycyl-D-valine bond hydrolysis is 267 years (with a range of 175-564 years).

Polypeptide, DNA fragment encoding the same, drug composition containing the same and process for producing the same

This invention particularly provides a novel polypeptide having high protease-inhibiting activity, preferably FXa-inhibiting activity, which comprises, at least as a part of the polypeptide, an amino acid sequence resulting from substitution of an amino acid for at least one amino acid in the following amino acid sequence (1), wherein the amino acid substitution is at least one substitution selected from the following substitution means (i) to (iii). It also provides a process for the production of the polypeptide, a novel DNA fragment encoding the polypeptide and a drug composition containing the same. Amino acid sequence (1) STR1 (i) Substitution of 15 position Gln counting from the N-terminus by an amino acid other than Gln. (ii) Substitution of 42 position Tyr counting from the N-terminus by an amino acid other than Tyr. (iii) Substitution of 7 position Arg counting from the N-terminus by an amino acid other than Arg.

Polypeptide, DNA fragment encoding the same, drug composition containing the same and process for producing the same

This invention particularly provides a novel polypeptide having high protease-inhibiting activity, preferably FXa-inhibiting activity, which comprises, at least as a part of the polypeptide, an amino acid sequence resulting from substitution of an amino acid for at least one amino acid in the following amino acid sequence (1), wherein the amino acid substitution is at least one substitution selected from the following substitution means (i) to (iii). It also provides a process for the production of the polypeptide, a novel DNA fragment encoding the polypeptide and a drug composition containing the same. ______________________________________Amino acid sequence (1)______________________________________Cys Asn Leu Pro Ile Val Arg Gly Pro CysArg Ala Phe Ile Gln Leu Trp Ala Phe AspAla Val Lys Gly Lys Cys Val Leu Phe ProTyr Gly Gly Cys Gln Gly Asn Gly Asn LysPhe Tyr Ser Glu Lys Glu Cys Arg Glu TyrCys______________________________________ (i) Substitution of 15 position Gln counting from the N-terminus by an amino acid other than Gln. (ii) Substitution of 42 position Tyr counting from the N-terminus by an amino acid other than Tyr. (iii) Substitution of 7 position Arg counting from the N-terminus by an amino acid other than Arg.