19542-54-2

Basic information

• Product Name: Z-VAL-VAL-OH
• Synonyms: Z-VAL-VAL-OH;Z-L-VALYL-L-VALINE
• CAS NO: 19542-54-2
• Molecular Formula: C₁₈H₂₆N₂O₅
• Molecular Weight: 350.41
• Mol File: 19542-54-2.mol
• Article Data: 9

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: Z-VAL-VAL-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Z-VAL-VAL-OH(19542-54-2)
• EPA Substance Registry System: Z-VAL-VAL-OH(19542-54-2)

Safety Data

• Hazardous Substances Data: 19542-54-2(Hazardous Substances Data)

Usage

General Description

"Z-VAL-VAL-OH" is a synthetic peptide containing the amino acids valine and an N-terminal benzyloxycarbonyl group. It is often used in research and pharmaceutical applications as a model substrate for studying enzyme activity, particularly in the field of proteases. The specific sequence and structure of "Z-VAL-VAL-OH" make it a valuable tool for investigating the mechanisms of peptide bond hydrolysis and the specificity of enzymes that catalyze such reactions. Additionally, its properties make it a useful component in the development and testing of new enzyme inhibitors and drug therapies. Overall, "Z-VAL-VAL-OH" plays a crucial role in advancing our understanding of enzyme function and in the development of new pharmaceutical compounds.

Upstream product

• 3918-94-3 Val-Val 
• 501-53-1 benzyl chloroformate 
• 516-06-3 D,L-valine 
• 4070-48-8 L-Valine methyl ester 
• 17431-03-7 L-valine ethyl ester 
• 17609-47-1 L-Valine ethyl ester hydrochloride 
• 1149-26-4 N-benzyloxycarbonylvaline 
• 6306-52-1 L-valine methylester hydrochloride 
• 1149-26-4 (S)-N-(benzyloxycarbonyl)valine 
• 72-18-4 L-valine 
• 10512-93-3 Z-Val-ONp 
• 3496-11-5 2,5-dioxopyrrolidin-1-yl (2S)-2-(((benzyloxy)carbonyl)amino)-3-methylbutanoate 
• 6479-43-2 N-Benzyloxycarbonyl-L-valyl-L-valin-diphenylmethylester 
• 55378-69-3 (S)-2-Benzyloxycarbonylamino-3-methyl-butyric acid 3-ethylcarbamoyl-2-hydroxy-phenyl ester 

Downstream Products

• 944919-83-9 Z-L-Val-L-Val-L-Glu(OtBu)OtBu 
• 135219-43-1 2-(2-{3-[2-(2-amino-3-methylbutyrylamino)-3-methyl-butyrylamino]-2-oxo-pentanoylamino}-4-methylpentanoylamino)-3-methylbutyric acid 
• 135219-44-2 2-(2-{3-[2-(2-benzyloxycarbonylamino-3-methylbutyrylamino)-3-methyl-butyrylamino]-2-oxo-pentanoylamino}-4-methylpentanoylamino)-3-methylbutyric acid benzyl ester 
• 874190-42-8 Z-Leu-Val-Val-Tyr-Pro 
• 874190-41-7 Val-Val-Tyr(tBu)-Pro-O-tBu 
• 852983-16-5 Z-Val-Val-Pro-Gln(Trt)-OH 
• 2471-53-6 Z-Val-Val-Val-OMe 
• 89092-73-9 Z-Val-Val-Gly-OMe 
• 188054-60-6 (1-{1-[1-[3-cyano-1-ethyl-2-oxo-3-(triphenyl-λ⁵-phosphanylidene)-propylcarbamoyl]-2-methylpropylcarbamoyl]-2-methylpropylcarbamoyl}-2-methylpropyl)-carbamic acid benzyl ester 
• 6479-43-2 N-Benzyloxycarbonyl-L-valyl-L-valin-diphenylmethylester 
• 128228-49-9 [(S)-1-((S)-4-Isopropyl-5-oxo-4,5-dihydro-oxazol-2-yl)-2-methyl-propyl]-carbamic acid benzyl ester 
• 3918-94-3 Val-Val 

Relevant articles and documents

Synthesis of all the stereoisomers of statine (4-amino-3-hydroxy-6-methylheptanoic acid). Inhibition of pepsin activity by N-carbobenzoxy-L-valyl-L-valyl-statine derived from the four stereoisomers.

Synthesis of all four stereoisomers of the novel amino acid statine, 4-amino-3-hydroxy-6-methylheptanoic acid, found in pepstatin, a potent acid protease inhibitor, has been accomplished. Carbobenzoxy-L-valyl-L-valyl-statine tripeptides derived from all f

Synthesis and properties of the retro-analogue of myelopeptide MP-2

The bone marrow myelopeptide MP-2 (Leu-Val-Val-Tyr-Pro-Trp), exhibiting antitumor activity, and its retro-analogue (Trp-Pro-Tyr-Val-Val-Leu) were synthesized, and their properties were studied. The in vitro and in vivo activities of retro-MP-2 were compar

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.