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16012-70-7

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16012-70-7 Usage

Chemical Properties

White to off-white powder

Check Digit Verification of cas no

The CAS Registry Mumber 16012-70-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,6,0,1 and 2 respectively; the second part has 2 digits, 7 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 16012-70:
(7*1)+(6*6)+(5*0)+(4*1)+(3*2)+(2*7)+(1*0)=67
67 % 10 = 7
So 16012-70-7 is a valid CAS Registry Number.
InChI:InChI=1/C14H18N2O5/c1-9(12(17)15-10(2)13(18)19)16-14(20)21-8-11-6-4-3-5-7-11/h3-7,9-10H,8H2,1-2H3,(H,15,17)(H,16,20)(H,18,19)

16012-70-7SDS

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 Z-ALA-ALA-OH

1.2 Other means of identification

Product number -
Other names N-Cbz-L-Ala-L-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:16012-70-7 SDS

16012-70-7Relevant articles and documents

Optimization and anti-cancer properties of fluoromethylketones as covalent inhibitors for ubiquitin C-terminal hydrolase L1

Chen, Hao,Das, Chittaranjan,Flaherty, Daniel P.,Galardy, Paul J.,Hewitt, Chad S.,Hussain, Sajjad,Imhoff, Ryan D.,Krabill, Aaron D.,Muli, Christine S.,Wendt, Michael K.

supporting information, (2021/05/31)

The deubiquitinating enzyme (DUB) UCHL1 is implicated in various disease states including neurodegenerative disease and cancer. However, there is a lack of quality probe molecules to gain a better understanding on UCHL1 biology. To this end a study was carried out to fully characterize and optimize the irreversible covalent UCHL1 inhibitor VAEFMK. Structure-activity relationship studies identified modifications to improve activity versus the target and a full cellular characterization was carried out for the first time with this scaffold. The studies produced a new inhibitor, 34, with an IC50 value of 7.7 μM against UCHL1 and no observable activity versus the closest related DUB UCHL3. The molecule was also capable of selectively inhibiting UCHL1 in cells and did not demonstrate any discernible off-target toxicity. Finally, the molecule was used for initial probe studies to assess the role of UCHL1 role in proliferation of myeloma cells and migration behavior in small cell lung cancer cells making 34 a new tool to be used in the biological evaluation of UCHL1.

Legumain Activated Doxorubicin Derivative as well as Preparation Method and Application Thereof

-

Paragraph 0041; 0044; 0045, (2019/05/18)

The present invention discloses doxorubicin derivatives for targeted activation by Legumain, its preparation method and use. The doxorubicin derivatives are obtained by condensation between the amino group of compound A and the carboxyl group of compound B and have the following structure: compounds A and B have the following structures, respectively: wherein R3 in compound B is Leu or absent; R4 is any one amino acid selected from the group consisting of Ala and Thr; R5 is any one amino acid selected from the group consisting of Ala, Thr and Asn; R6 is wherein n=1-20; or wherein R7 is substituted or unsubstituted, linear or branched, saturated or unsaturated C1-C20 fatty hydrocarbon, or substituted or unsubstituted C6-C20 aromatic hydrocarbon. The doxorubicin derivatives of the present invention are specifically tumor-targeted and have a long in vivo metabolic half-life, as compared with doxorubicin. They exhibit an efficient and safe anti-tumor effect and could be used to prepare an anti-tumor drug.

Legumain Activated Doxorubicin Derivative as well as Preparation Method and Application Thereof

-

Paragraph 0041; 0044; 0045, (2017/05/07)

The present invention discloses doxorubicin derivatives for targeted activation by Legumain, its preparation method and use. The doxorubicin derivatives are obtained by condensation between the amino group of compound A and the carboxyl group of compound B and have the following structure: compounds A and B have the following structures, respectively: wherein R3 in compound B is Leu or absent; R4 is any one amino acid selected from the group consisting of Ala and Thr; R5 is any one amino acid selected from the group consisting of Ala, Thr and Asn; R6 is wherein n=1-20; or wherein R7 is substituted or unsubstituted, linear or branched, saturated or unsaturated C1-C20 fatty hydrocarbon, or substituted or unsubstituted C6-C20 aromatic hydrocarbon. The doxorubicin derivatives of the present invention are specifically tumor-targeted and have a long in vivo metabolic half-life, as compared with doxorubicin. They exhibit an efficient and safe anti-tumor effect and could be used to prepare an anti-tumor drug.

SPECIFICALLY ACTIVATED MICROMOLECULAR TARGET COUPLING BODY IN TUMOR MICROENVIRONMENT AND USE THEREOF

-

Paragraph 0080; 0083; 0084; 0227; 0229, (2017/07/14)

Provided are an anticancer compound comprising a cleavable linker specifically activated in a tumor microenvironment, and use thereof. The anticancer compound is represented by the following formula, wherein, R1 is a normal functional group or a protection group; R2 is Ala, Thr, Val or Ile; R3 is Ala, Val or Asn; R4 is a drug group linked via a hydroxyl group or an amino group; and the general formula of the drug is R4H. The anticancer compound is only activated at a local portion of a tumor, thus avoiding the defect of immune system damage of a traditional chemotherapeutic drug, and promoting tumor immunization by removing a tumor immunosuppression cell. The anticancer compound or pharmaceutical composition thereof is jointly used with immunotherapy, thus improving the effect of treating the tumor, and effectively inhibiting tumor metastasis and osseous metastasis.

Carboxypeptidase from Streptomyces bikiniensis: Primary structure, isolation, and properties

Serkina,Zalunin,Levitin,Voejkova,Tyaglov,Novikova,Emeljanova,Konstantinova,Chestukhina

experimental part, p. 1032 - 1038 (2011/11/06)

A metallocarboxypeptidase produced by Streptomyces bikiniensis 27 strain (VKPM Ac-1783) (CPSb) was purified and characterized. The enzyme cleaves both basic and hydrophobic C-terminal amino acid residues from synthetic peptides, that is, it possesses specificity of mammalian carboxypeptidases A and B. The enzyme also hydrolyzes peptides bearing glutamic acid at the C-end. CPSb exhibits its maximal activity at pH 7.0-7.6 and 55°C. The nucleotide sequence encoding the mature CPSb in S. bikiniensis 27 (VKPM Ac-1783) genome (Accession No. GU362077) was determined. It is shown that the primary structure of the mature enzyme has a moderate degree of identity with orthologs from Streptomyces griseus (79% identity) and Streptomyces avermitilis (85% identity).

Synthesis of peptide aldehydes via enzymatic acylation of amino aldehyde derivatives

Voyushina, Tatiana L.,Potetinova, Joanna V.,Milgotina, Ekaterina I.,Stepanov, Valentin M.

, p. 2953 - 2959 (2007/10/03)

Two ways for semi-enzymatic preparation of the peptide aldehydes are proposed: (1) enzymatic acylation of amino alcohols with acyl peptide esters and subsequent chemical oxidation of the resulting peptide alcohols with DMSO/acetic anhydride mixture or (2) enzymatic acylation of the preliminarily obtained by a chemical route amino aldehyde semicarbazones. Subtilisin 72, serine proteinase with a broad specificity, distributed over macroporous silica, was used as a catalyst in both cases. Due to the practical absence of water in the reaction mixtures the yields of the products in both enzymatic reactions were nearly quantitative. The second way seems to be more attractive because all chemical stages were carried out with amino acid derivatives, far less valuable compounds than peptide ones. A series of peptide aldehydes of general formula Z-Ala-Ala-Xaa-al (where Xaa-al=leucinal, phenylalaninal, alaninal, valinal) was obtained. The inhibition parameters for these compounds, in the hydrolysis reactions of corresponding chromogenic substrates for subtilisin and α-chymotrypsin, were determined. Copyright (C) 1999 Elsevier Science Ltd.

Characterization of acyl adenyl anhydrides: Differences in the hydrolytic rates of fatty acyl-AMP and aminoacyl-AMP derivatives

Schall, Otto F.,Suzuki, Iwao,Murray, Clare L.,Gordon, Jeffrey I.,Gokel, George W.

, p. 8661 - 8667 (2007/10/03)

An improved procedure has been developed to prepare RCOOPO2-Ado (R = C6H13 and C15H31), the intermediate in the enzymatic synthesis of acyl-CoA's. The product has been characterized by spectral methods which, in turn, were used to define the hydrolysis rates of RCO-AMP. When R is a fatty acyl group, the hydrolysis rate is 10-fold slower than when R is aminoacyl. In both cases, the hydrolysis rate is enhanced by Mg2+. We speculate that the rate acceleration is due to intramolecular participation of the second carbonyl group in the aminoacyl residue.

Selective deprotection of phenacyl, benzyl and methyl esters of N-protected amino acids and dipeptides and N-protected amino acids benzyl ester linked to resins with bis(tributyltin) oxide

Salomon, Claudio J.,Mata, Ernesto G.,Mascaretti, Oreste A.

, p. 995 - 999 (2007/10/03)

Phenacyl, methyl and benzyl esters of various N-α-Boc, N-α-Cbz or N,N-dimethylamino protected amino acids and dipeptides, as well as esters of N-α-protected amino acids linked to Wang and Pam resins have been efficiently and chemoselectively cleaved by bis(tributyltin) oxide in aprotic solvents to give the corresponding carboxylic acids in good yields. Moreover, the absence of racemization during the deprotection has been demonstrated. A limitation of the method is the instability of the N-ε-Fmoc group in the amino acid esters 8 and 10, N-α-Fmoc-L-alanine linked to Wang resin 23 and the Cbz protecting groups in N-α-Boc-N-ε-Cbz-L-lysine benzyl and methyl esters (5 and 7), respectively, and N-α-Cbz-L-alanyl-L-alanine methyl ester 19. In the case of N-α-protected dipeptides, there was no evidence of free amino acid which indicates that the peptide bond is unaffected.

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