10342-47-9

Basic information

• Product Name: L-Phenylalanine, N-L-valyl-, methyl ester, monohydrochloride
• CAS NO: 10342-47-9
• Molecular Formula: C15H22N2O3.ClH
• Molecular Weight: 314.812
• Mol File: 10342-47-9.mol
• Article Data: 7

Chemical Properties

• CAS DataBase Reference: L-Phenylalanine, N-L-valyl-, methyl ester, monohydrochloride(CAS DataBase Reference)
• NIST Chemistry Reference: L-Phenylalanine, N-L-valyl-, methyl ester, monohydrochloride(10342-47-9)
• EPA Substance Registry System: L-Phenylalanine, N-L-valyl-, methyl ester, monohydrochloride(10342-47-9)

Safety Data

• Hazardous Substances Data: 10342-47-9(Hazardous Substances Data)

Upstream product

• 78581-05-2 For-Val-Phe-OMe 
• 116763-17-8 (S)-3-methyl-2-(1-pyrrolyl)butyryl-L-phenylalanine methyl ester 
• 67-56-1 methanol 
• 3918-92-1 L-valyl L-phenylalanine 
• 72-18-4 L-valine 
• 63813-68-3 (2S)-3-methyl-2-(1H-pyrrol-1-yl)butanoic acid 
• 63-91-2 L-phenylalanine 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 141468-55-5 4-isopropyl-2,5-dioxo-oxazolidine-3-carboxylic acid-tert-butyl ester 
• 20902-47-0 N-tert-butoxycarbonyl-L-valyl-L-phenylalanine methyl ester 
• 4289-97-8 N-formyl-L-valine 

Downstream Products

• 1431295-89-4 Boc-Trp-Val-Phe-OMe 
• 1447815-56-6 L-isoseryl-L-valyl-L-phenylalanine 
• 1333311-06-0 (S)-2-((S)-2-(2-(2-acetamidophenyl)-2-oxoacetamido)-3-methylbutanamido)-3-phenylpropanoic acid 
• 1333311-12-8 (S)-dimethyl 2-((S)-2-((S)-2-(2-(2-acetamidophenyl)-2-oxoacetamido)-3-methylbutanamido)-3-phenylpropanamido)pentanedioate 
• 1021907-05-0 C₄₈H₅₂N₆O₁₂ 
• 1021906-84-2 C₂₅H₂₈BrN₃O₆ 
• 1021906-87-5 C₂₆H₃₁N₃O₆ 
• 1021906-81-9 (S)-methyl 2-((S)-2-(2-(2-acetamidophenyl)-2-oxoacetamido)-3-methylbutanamido)-3-phenylpropanoate 
• 1021907-06-1 C₅₀H₅₆N₆O₁₂ 
• 81322-89-6 (S)-2-{(S)-2-[(2S,3S)-3-((S)-2-Amino-4-methyl-pentanoylamino)-2-hydroxy-5-methyl-hexanoylamino]-3-methyl-butyrylamino}-3-phenyl-propionic acid methyl ester; hydrochloride 
• 81322-89-6 (S)-2-{(S)-2-[(2R,3S)-3-((S)-2-Amino-4-methyl-pentanoylamino)-2-hydroxy-5-methyl-hexanoylamino]-3-methyl-butyrylamino}-3-phenyl-propionic acid methyl ester; hydrochloride 

Relevant articles and documents

Site-Selective Acylation of Pyranosides with Oligopeptide Catalysts

Herein, we report the oligopeptide-catalyzed site-selective acylation of partially protected monosaccharides. We identified catalysts that invert site-selectivity compared to N-methylimidazole, which was used to determine the intrinsic reactivity, for 4,6

Design, synthesis and biological evaluation of novel L-isoserine tripeptide derivatives as aminopeptidase N inhibitors

Aminopeptidase N (APN/CD13) is one of the essential proteins for tumour invasion, angiogenesis and metastasis as it is over-expressed on the surface of different tumour cells. Based on our previous work that L-isoserine dipeptide derivatives were potent APN inhibitors, we designed and synthesized L-isoserine tripeptide derivatives as APN inhibitors. Among these compounds, one compound 16l (IC50=2.51±0.2 M) showed similar inhibitory effect compared with control compound Bestatin (IC50=6.25±0.4 M) and it could be used as novel lead compound for the APN inhibitors development as anticancer agents in the future.

Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: A strategy for the design of peptidase inhibitors

The cholecystokinin-8 (CCK-8)-inactivating peptidase is a serine peptidase which has been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10). It cleaves the neurotransmitter CCK-8 sulfate at the Met-Gly bond to give Asp-Tyr(SO3H)-Met-OH + Gly-Trp-Met-Asp-Phe-NH2. In seeking a reversible inhibitor of this peptidase, the enzymatic binding subsites were characterized using a fluorimetric assay based on the hydrolysis of the artificial substrate Ala-Ala-Phe-amidomethylcoumarin. A series of di- and tripeptides having various alkyl or aryl side chains was studied to determine the accessible volume for binding and to probe the potential for hydrophobic interactions. From this initial study the tripeptides Ile-Pro-Ile-OH (K(i) = 1 μM) and Ala-Pro-Ala-OH (K(i) = 3 μM) and dipeptide amide Val-Nvl-NHBu (K(i) = 3 μM) emerged as leads. Comparison of these structures led to the synthesis of Val-Pro-NHBu (K(i) = 0.57 μM) which served for later optimization in the design of butabindide, a potent reversible competitive and selective inhibitor of the CCK-8-inactivating peptidase. The strategy for this work is explicitly described since it illustrates a possible general approach for peptidase inhibitor design.