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Valylalanine, a dipeptide consisting of the amino acids valine and alanine, is a non-proteinogenic amino acid that does not get incorporated into proteins but may possess specific biological functions. Its unique properties and potential health benefits have garnered interest for its therapeutic uses and applications in various industries.

1115-74-8

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1115-74-8 Usage

Uses

Used in Pharmaceutical Industry:
Valylalanine is used as a therapeutic agent for its potential role in the treatment of neurodegenerative diseases. Its specific biological functions may contribute to mitigating the effects of such conditions.
Used in Anti-Inflammatory Applications:
Valylalanine is utilized as an anti-inflammatory agent, potentially offering relief in conditions characterized by inflammation due to its unique properties.
Used in Food Industry:
Valylalanine is employed as a functional ingredient in the food industry, capitalizing on its potential health benefits and unique characteristics to enhance or differentiate food products.
Used in Research:
Valylalanine serves as a subject of study in biological and medical research, aiming to further understand its biological activities, potential health benefits, and applications in various fields.
Further research is essential to fully explore the capabilities and potential uses of valylalanine, expanding its applications and benefits across different industries.

Check Digit Verification of cas no

The CAS Registry Mumber 1115-74-8 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,1,1 and 5 respectively; the second part has 2 digits, 7 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 1115-74:
(6*1)+(5*1)+(4*1)+(3*5)+(2*7)+(1*4)=48
48 % 10 = 8
So 1115-74-8 is a valid CAS Registry Number.

1115-74-8SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name 2-[(2-amino-3-methylbutanoyl)amino]propanoic acid

1.2 Other means of identification

Product number -
Other names H-VAL-ALA-OH

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:1115-74-8 SDS

1115-74-8Downstream Products

1115-74-8Relevant academic research and scientific papers

SUBSTITUTED NAPHTHYRIDINONE COMPOUNDS USEFUL AS T CELL ACTIVATORS

-

Page/Page column 263, (2020/01/24)

Disclosed are compounds of Formula (I) or a salt thereof, wherein: R1, R2, R3, R4, R5, and m are defined herein. Also disclosed are methods of using such compounds to inhibit the activity of one or both of diacylglycerol kinase alpha (DGKα) and diacylglycerol kinase zeta (DGKζ), and pharmaceutical compositions comprising such compounds. These compounds are useful in the treatment of viral infections and proliferative disorders, such as cancer.

Coupling-Reagent-Free Synthesis of Dipeptides and Tripeptides Using Amino Acid Ionic Liquids

Furukawa, Shinya,Fukuyama, Takahide,Matsui, Akihiro,Kuratsu, Mai,Nakaya, Ryotaro,Ineyama, Takashi,Ueda, Hiroshi,Ryu, Ilhyong

supporting information, p. 11980 - 11983 (2015/08/18)

A general method for the synthesis of dipeptides has been developed, which does not require any coupling reagents. This method is based on the reaction of readily available HCl salts of amino acid methyl esters with tetrabutylphosphonium amino acid ionic liquids. The isolation procedure of stepwise treatment with AcOH is easy to carry out. The method was extended to the synthesis of tripeptide, tyrosyl-glycyl-glycine, present in IMREG-1, also.

Synthesis and NMR elucidation of pentacycloundecane-derived hydroxy acid peptides as potential anti-HIV-1 agents

Karpoormath, Rajshekhar,Albericio, Fernando,Govender, Thavendran,Maguire, Glenn E. M.,Kruger, Hendrik G.

, p. 1461 - 1471 (2013/10/22)

The synthesis and NMR elucidation of eight novel peptides incorporating the pentacycloundecane (PCU)-derived hydroxy acid are reported. The PCU cage amino acids were synthesized as racemates and the incorporation of the PCU-derived hydroxy acid with natural (S)-amino acids produced inseparable diastereomeric peptides. A series of overlapping signals from the cage and that of the peptide side chain was observed in the 1H- and 13C-NMR spectra, complicating the elucidation thereof. Two-dimensional NMR techniques proved to be a very useful tool in overcoming these difficulties. These compounds are potential HIV protease inhibitors.

Pentacycloundecane derived hydroxy acid peptides: A new class of irreversible non-scissile ether bridged type isoster as potential HIV-1 wild type C-SA protease inhibitors

Karpoormath, Rajshekhar,Sayed, Yasien,Govender, Patrick,Govender, Thavendran,Kruger, Hendrik G.,Soliman, Mahmoud E.S.,Maguire, Glenn E.M.

experimental part, p. 19 - 29 (2012/03/26)

Novel peptides incorporating the PCU derived hydroxy acid (5-hydroxy-4-oxahexacyclo[5.4.1.02,6.03,10.0 5,9.08,11]dodecane) were synthesized and their activity against the resistance-prone wild type C-South African (C-SA) HIV-protease is reported. The attachment of peptides and peptoids to the PCU derived hydroxy acid resulted in a series of structurally diverse promising HIV-1 protease inhibitors. Amongst the nine novel compounds, 16, 17, 20 and 23 gave IC 50 values ranging from 0.6 to 5.0 μM against the wild type C-SA HIV-1 protease enzyme. Docking studies and molecular dynamic (MD) simulations have been carried out in order to understand the binding mode of the PCU moiety at the active site of the HIV protease enzyme. A conserved hydrogen bonding pattern between the PCU derived hydroxy ether and the active site residues, ASP25/ASP25′, was observed in all active compounds.

PYRROLOBENZODIAZEPINES AND CONJUGATES THEREOF

-

, (2011/10/31)

Conjugates and compounds for making conjugates which are PBD molecules linked via the N10 position are disclosed, along with the use of the conjugates for treating proliferative diseases, including cancer.

The small peptide-catalyzed direct asymmetric aldol reaction in water

Dziedzic, Pawel,Zou, Weibiao,Hafren, Jonas,Cordova, Armando

, p. 38 - 40 (2007/10/03)

The asymmetric aldol reaction is a powerful method for forming carbon-carbon bonds. Small peptides with a primary amine as the catalytic residue catalyze asymmetric aqueous aldol reactions between unmodified ketones and aldehydes to furnish the corresponding aldol products with high ees. The high momodularity of the small peptides should enable the construction of several novel catalysts by combinatorial techniques for the aqueous asymmetric aldol reaction. The remarkably high difference in stereoselectivity between the peptide bond-formation was an important step towards the evaluation of asymmetric catalysis and homochilarity.

Direct asymmetric intermolecular aldol reactions catalyzed by amino acids and small peptides

Cordova, Armando,Zou, Weibiao,Dziedzic, Pawel,Ibrahem, Ismail,Reyes, Efraim,Xu, Yongmei

, p. 5383 - 5397 (2008/02/13)

In nature there are at least nineteen different acyclic amino acids that act as the building blocks of poly-peptides and proteins with different functions. Here we report that α-amino acids, β-amino acids, and chiral amines containing primary amine functions catalyze direct asymmetric intermolecular aldol reactions with high enantio-selectivities. Moreover, the amino acids can be combined into highly modular natural and unusual small peptides that also catalyze direct asymmetric intermolecular aldol reactions with high stereoselectivities, to furnish the corre sponding aldol products with up to > 99% ee. Simple amino acids and small peptides can thus catalyze asymmetric aldol reactions with stereoselectivities matching those of natural enzymes that have evolved over billions of years. A small amount of water accelerates the asymmetric aldol reactions catalyzed by amino acids and small peptides, and also increases their stereoselectivities. Notably, small peptides and amino acid tetrazoles were able to catalyze direct asymmetric aldol reactions with high enantioselectivities in water, while the parent amino acids, in stark contrast, furnished nearly racemic products. These results suggest that the prebiotic oligomerization of amino acids to peptides may plausibly have been a link in the evolution of the homochirality of sugars. The mechanism and stereochemistry of the reactions are also discussed.

Small peptides as modular catalysts for the direct asymmetric aldol reaction: Ancient peptides with aldolase enzyme activity

Zou, Weibiao,Ibrahem, Ismail,Dziedzic, Pawel,Sunden, Henrik,Cordova, Armando

, p. 4946 - 4948 (2007/10/03)

Simple peptides and their analogues having a primary amino group as the catalytic residue mediate the direct asymmetric intermolecular aldol reaction with high stereoselectivity and furnish the corresponding aldol products with up to 99% ee; this intrinsic ability of highly modular peptides may explain the initial molecular evolution of aldolase enzymes. The Royal Society of Chemistry 2005.

The Steric Hindrance of the Stepwise Reaction of N-Carboxy α-Amino Acid Anhydride with the α-Amino Acid Ester

Oya, Masanao,Takahashi, Tomoko

, p. 2705 - 2707 (2007/10/02)

The mechanisms of the reactions of 4-alkyloxazolidinediones (1) (N-carboxy α-amino acid anhydrides(NCAs)) with α-amino acid benzyl ester p-toluenesulfonates (2) were investigated in acetonitrile containing triethylamine at low and room temperatures.Two types of reactions were observed: (1) the polymerization of NCAs was initiated with a small amount of 2 to produce polypeptides (6), and (2) the dipeptide benzyl esters (4) were produced by the stepwise reaction of NCAs with the esters.Both the polymerization and the dipeptide formation (1+2) seemed to be initiated by the nucleophilic attack of the amino group of the ester on the C-5 carbon of NCAs.The polymerization proceeded when the side chains of the amino acid esters (R2) were more bulky than those of the NCAs (R1).On the contrary, dipeptide esters were produced when the side chains of the NCAs (R1) were more bulky than those of the esters (R2).

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