128647-50-7

Usage

Uses

Used in Pharmaceutical Industry:
(S)-Benzyl (3-Methyl-1-(MethylaMino)-1-oxobutan-2-yl)carbaMate is used as a chemical intermediate for the synthesis of medications, contributing to the development of new pharmaceutical compounds with potential therapeutic effects.
Used in Chemical Compounds Synthesis:
In the field of organic chemistry, (S)-Benzyl (3-Methyl-1-(MethylaMino)-1-oxobutan-2-yl)carbaMate serves as a building block for the creation of other complex chemical compounds, expanding the scope of chemical research and innovation.

Upstream product

• 1149-26-4 (S)-N-(benzyloxycarbonyl)valine 
• 593-51-1 methylamine hydrochloride 
• 74-89-5 methylamine 
• 3496-11-5 2,5-dioxopyrrolidin-1-yl (2S)-2-(((benzyloxy)carbonyl)amino)-3-methylbutanoate 
• 41445-88-9 Z-Val-OCO₂ⁱBu 

Downstream Products

• 87105-26-8 L-valine N-methylamide 
• 74410-26-7 (S)-2-amino-N,3-dimethylbutanamide hydrochloride 
• 264887-80-1 N-benzyloxycarbonyl-L-valyl-L-valine methylamide 
• 213895-50-2 B268 
• 416899-42-8 {[(S)-3-Methyl-1-((S)-2-methyl-1-methylcarbamoyl-propylcarbamoyl)-butylcarbamoyl]-methyl}-carbamic acid benzyl ester 
• 416899-41-7 {[(S)-1-((S)-2-Methyl-1-methylcarbamoyl-propylcarbamoyl)-ethylcarbamoyl]-methyl}-carbamic acid benzyl ester 
• 416899-38-2 [(S)-3-Methyl-1-((S)-2-methyl-1-methylcarbamoyl-propylcarbamoyl)-butyl]-carbamic acid benzyl ester 
• 416899-37-1 [(S)-1-((S)-2-Methyl-1-methylcarbamoyl-propylcarbamoyl)-ethyl]-carbamic acid benzyl ester 

Relevant academic research and scientific papers

A noncovalent approach to antiparallel β-sheet formation

Four tripeptide chains, when attached to the same end of a hydrogen-bonded duplex (1.2) with the unsymmetrical, complementary sequences of ADAA/DADD, have been brought into proximity, leading to the formation of four hybrid duplexes, 1a·2a, 1a·2b, 1b·2a,

Antiviral protease inhibitors

Compounds of the formula I: wherein: A′ and A″ are independently the same or different group of the formula II: wherein: R′ is H. CH3, C(CH3)2, —ORa, —N(Ra)2, —N(Ra)ORa/sup

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.

Design and synthesis of new potent C2-symmetric HIV-1 protease inhibitors. Use of L-mannaric acid as a peptidomimetic scaffold

A study on the use of derivatized carbohydrates as C2-symmetric HIV-1 protease inhibitors has been undertaken. L-Mannaric acid (6) was bis-O- benzylated at C-2 and C-5 and subsequently coupled with amino acids and amines to give C2-s

Activation of carboxylic acids by pyrocarbonates: Synthesis of alkylamides of N-protected amino acids

Alkylamides of amino acids were prepared with high yields via activation of N-protected amino acids by di-tert-butyl pyrocarbonate-pyridine reagent in the presence of alkylamine hydrochlorides and potassium hydrocarbonate.

Conformational Investigations of α,β-Dehydropeptides. I. Synthesis of Model Dipeptides

Three series of model dipeptides: Ac-Pro-X-NHMe, where X = L-, D- and Δ-Ala, L-, D- and (Z)-Δ-Phe and L-, D- and Δ-Val, designed for conformational investigation of α,β-dehydroamino acid effect on peptide chain β-turn have been synthesized.