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2766-18-9

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2766-18-9 Usage

General Description

Z-PRO-GLY-OH is a chemical compound that consists of three components: Z, Pro, and Gly. The Z component is a protecting group for the amino group of proline, which is an important amino acid in the body. The Pro component refers to proline, a non-essential amino acid that is involved in the synthesis of collagen, connective tissues, and muscle. The Gly component stands for glycine, another non-essential amino acid that plays a crucial role in the synthesis of proteins and the functioning of the central nervous system. Z-PRO-GLY-OH is likely a peptide or an intermediate compound used in the synthesis of peptides, proteins, or other biologically active molecules. It may have applications in the fields of biochemistry, pharmaceuticals, and medical research.

Check Digit Verification of cas no

The CAS Registry Mumber 2766-18-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,7,6 and 6 respectively; the second part has 2 digits, 1 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 2766-18:
(6*2)+(5*7)+(4*6)+(3*6)+(2*1)+(1*8)=99
99 % 10 = 9
So 2766-18-9 is a valid CAS Registry Number.
InChI:InChI=1/C15H18N2O5/c18-13(19)9-16-14(20)12-7-4-8-17(12)15(21)22-10-11-5-2-1-3-6-11/h1-3,5-6,12H,4,7-10H2,(H,16,20)(H,18,19)

2766-18-9SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 16, 2017

Revision Date: Aug 16, 2017

1.Identification

1.1 GHS Product identifier

Product name Z-PRO-GLY-OH

1.2 Other means of identification

Product number -
Other names Z-L-ProGly-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:2766-18-9 SDS

2766-18-9Relevant articles and documents

Organocatalyzed Asymmetric Aldol Reaction of α-Keto Amides with A Tripeptide Catalyst

Kon, Kazumasa,Takai, Hiromu,Kobayashi, Takumu,Kohari, Yoshihito,Murata, Miki

supporting information, p. 829 - 832 (2021/02/26)

An organocatalyzed asymmetric aldol reaction of α-keto amides was developed. An N-terminal 4- trans -siloxyproline-based tripeptide with an l - tert -leucine unit adjacent to the 4- trans -siloxyproline residue was used to catalyze the reaction between various α-keto amides and acetone, to produce the corresponding aldol adducts with up to 99% yield and 91% ee.

One-step C-terminal deprotection and activation of peptides with peptide amidase from stenotrophomonas maltophilia in neat organic solvent

Arif, Muhammad I.,Toplak, Ana,Szymanski, Wiktor,Feringa, Ben L.,Nuijens, Timo,Quaedflieg, Peter J. L. M.,Wu, Bian,Janssen, Dick B.

, p. 2197 - 2202 (2014/07/21)

Chemoenzymatic peptide synthesis is a rapidly developing technology for cost effective peptide production on a large scale. As an alternative to the traditional C→N strategy, which employs expensive N-protected building blocks in each step, we have investigated an N→C extension route that is based on activation of a peptide C-terminal amide protecting group to the corresponding methyl ester. We found that this conversion is efficiently catalysed by Stenotrophomonas maltophilia peptide amidase in neat organic media. The system excludes the possibility of internal peptide cleavage as the enzyme lacks intrinsic protease activity. The produced peptide methyl ester was used for peptide chain extension in a kinetically controlled reaction by a thermostable protease.

Synthesis and in vitro evaluation of macromolecular antitumour derivatives based on phenylenediamine mustard

De Winne, Katleen,Seymour, Leonard W.,Schacht, Etienne H.

, p. 159 - 168 (2007/10/03)

Poly-[N-(2-hydroxyethyl)-l-glutamine] (PHEG) and poly(ethylene glycol) (PEG)-grafted PHEG conjugates of N,N-di(2-chloroethyl)-4-phenylenediamine mustard (PDM) were synthetised. A collagenase-sensitive oligopeptide spacer was selected to link the cytotoxic agent PDM onto the polymeric carrier. First, the oligopeptide-drug conjugate, l-pro-l-leu-gly-l-pro-gly-PDM, was prepared. In a second step, the low molecular weight PDM derivative and PEG-NH2 were coupled to a N,N-disuccinimidylcarbonate activated PHEG. Dynamic laser light scattering measurements indicated the formation of aggregates. The presence of human serum albumin had no significant effect on the diameter of the conjugates. The hydrolytic stability of the conjugates was investigated in buffer solutions. The conjugates showed an improved stability compared to the parent nitrogen mustard. The enzymatic degradation studies of the polymeric conjugates were performed in the presence of collagenase type IV (Clostridiopeptidase A; EC 3.4.24.3), cathepsin B (EC 3.4.22.1), cathepsin D (EC 3.4.23.5) and tritosomes. Only the bacterial collagenase type IV was able to cleave the spacer releasing free PDM and its peptidyl derivative, gly-l-pro-gly-PDM. The in vitro cytotoxicity of the conjugates was evaluated against HT1080 fibrosarcoma cells and MDA adenocarcinoma cells. All conjugates showed low toxicity towards these cell lines.

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