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4033-42-5

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4033-42-5 Usage

General Description

AC-LEU-GLY-OH is a chemical compound consisting of the amino acids acetyl-leucine and glycine linked together, with a hydroxyl group at the carboxylic acid end. It is commonly used in molecular biology and biochemistry research as a building block for peptide synthesis and as a standard for analyzing the performance of chromatography columns. AC-LEU-GLY-OH is also used in pharmaceutical research for the development of drug candidates, particularly in the design of peptide-based therapeutics. Additionally, it can be utilized in the development of new materials and as a component in the production of flavor enhancers and food additives. Overall, AC-LEU-GLY-OH plays diverse roles in various scientific and industrial applications, making it a valuable and versatile chemical compound.

Check Digit Verification of cas no

The CAS Registry Mumber 4033-42-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 4,0,3 and 3 respectively; the second part has 2 digits, 4 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 4033-42:
(6*4)+(5*0)+(4*3)+(3*3)+(2*4)+(1*2)=55
55 % 10 = 5
So 4033-42-5 is a valid CAS Registry Number.

4033-42-5Relevant articles and documents

Substrates for efficient fluorometric screening employing the NAD-dependent sirtuin 5 lysine deacylase (KDAC) enzyme

Madsen, Andreas S.,Olsen, Christian A.

, p. 5582 - 5590 (2012/09/21)

The class III lysine deacylases (KDACs), also known as the sirtuins, have emerged as interesting drug targets for therapeutic intervention in a variety of diseases. To gain a deeper understanding of the processes affected by sirtuins, the development of selective small molecule modulators of individual isozymes has been a longstanding goal. Essential for the discovery of novel modulators, however, are good screening protocols and mechanistic insights with regard to the targets in question. We therefore evaluated the activities of the seven human sirtuin hydrolases against a panel of fluorogenic substrates. Both commonly used, commercially available substrates and novel chemotypes designed to address recent developments in the field of lysine post-translational modification were evaluated. Our investigations led to the discovery of two new fluorogenic ε-N-succinyllysine-containing substrates that enable highly efficient and enzyme-economical screening employing sirtuin 5 (SIRT5). Furthermore, optimized protocols for facile kinetic investigations were developed, which should be valuable for enzyme kinetic investigations. Finally, these protocols were applied to a kinetic analysis of the inhibition of SIRT5 by suramin, a potent sirtuin inhibitor previously shown by X-ray crystallography to bind the substrate pocket of the human SIRT5 KDAC enzyme.

Design and synthesis of a new series of amphiphilic peptide-β- cyclodextrins as phase transfer carriers for glucosamine

Seyedi, Seyed Mohammad,Sadeghian, Hamid,Jabbari, Atena,Assadi, Amir,Momeni, Hamideh

experimental part, p. 6754 - 6760 (2010/10/01)

A new series of amphiphilic β-cyclodextrins were designed and synthesized by grafting peptide chains on to all primary hydroxyl groups via ester bond formation. The desired amphiphilic structures have been produced from ester connection between the C-6 of β-cyclodextrin and the carboxyl group of N-acetylated resides: H2N-Leu-COOH, H2N-Leu-Gly-COOH, H2N-Leu-Gly-Leu-COOH, and H2N-Leu-Gly-Leu-Gly-COOH (3a-d). The synthetic pathway involves selective bromination of all primary hydroxyls of β-cyclodextrins and then substitution with the carboxylate moiety of the mentioned N-acetyl residues in the presence of DBU (1,8-diazabicyclo[5,4,0] undec-7-ene). The ability of the synthetic compounds for extraction and phase transfer of glucosamine, as a hydrophilic organic compound, was then studied. The results showed a considerable ability of these amphiphilic compounds for extraction and a selective tendency of 3c for phase transfer of glucosamine.

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