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3705-42-8

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  • China Biggest Factory & Manufacturer supply Cbz-L-Glutamic acid 1-benzyl ester CAS: 3705-42-8

    Cas No: 3705-42-8

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3705-42-8 Usage

Chemical Properties

White Solid

Uses

Different sources of media describe the Uses of 3705-42-8 differently. You can refer to the following data:
1. N-Benzyloxycarbonyl-L-glutamic acid 1-benzyl ester used as a potential neuroprotective agent.
2. A new glutamate analogue as potential neuroprotective agent.

Check Digit Verification of cas no

The CAS Registry Mumber 3705-42-8 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 3,7,0 and 5 respectively; the second part has 2 digits, 4 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 3705-42:
(6*3)+(5*7)+(4*0)+(3*5)+(2*4)+(1*2)=78
78 % 10 = 8
So 3705-42-8 is a valid CAS Registry Number.
InChI:InChI=1/C20H21NO6/c22-18(23)12-11-17(19(24)26-13-15-7-3-1-4-8-15)21-20(25)27-14-16-9-5-2-6-10-16/h1-10,17H,11-14H2,(H,21,25)(H,22,23)/t17-/m0/s1

3705-42-8 Well-known Company Product Price

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  • TCI America

  • (B3989)  1-Benzyl N-Carbobenzoxy-L-glutamate  >98.0%(HPLC)(T)

  • 3705-42-8

  • 5g

  • 740.00CNY

  • Detail
  • TCI America

  • (B3989)  1-Benzyl N-Carbobenzoxy-L-glutamate  >98.0%(HPLC)(T)

  • 3705-42-8

  • 25g

  • 2,490.00CNY

  • Detail
  • Alfa Aesar

  • (H62975)  N-Benzyloxycarbonyl-L-glutamic acid 1-benzyl ester, 95%   

  • 3705-42-8

  • 5g

  • 293.0CNY

  • Detail
  • Alfa Aesar

  • (H62975)  N-Benzyloxycarbonyl-L-glutamic acid 1-benzyl ester, 95%   

  • 3705-42-8

  • 25g

  • 1168.0CNY

  • Detail

3705-42-8SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 11, 2017

Revision Date: Aug 11, 2017

1.Identification

1.1 GHS Product identifier

Product name (4S)-5-oxo-5-phenylmethoxy-4-(phenylmethoxycarbonylamino)pentanoic acid

1.2 Other means of identification

Product number -
Other names N-Cbz-Glu-OBn

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:3705-42-8 SDS

3705-42-8Relevant articles and documents

The critical role of the aldehyde dehydrogenase PauC in spermine, spermidine, and diaminopropane toxicity in Pseudomonas aeruginosa: Its possible use as a drug target

Aguilera-Cruz, Alejandro,Cardona-Cardona, Yudy V.,Carrillo-Campos, Javier,Juárez-Díaz, Javier Andrés,López-Ortiz, Manuel,Mújica-Jiménez, Carlos,Mu?oz-Clares, Rosario A.,Regla, Ignacio

, (2021/11/30)

The opportunistic human pathogen Pseudomonas aeruginosa exhibits great resistance to antibiotics; so, new therapeutic agents are urgently needed. Since polyamines levels are incremented in infected tissues, we explored whether the formation of a toxic aldehyde in polyamines degradation can be exploited in combating infection. We cloned the gene encoding the only aminoaldehyde dehydrogenase involved in P. aeruginosa polyamines-degradation routes, PaPauC, overexpressed this enzyme, and found that it oxidizes 3-aminopropionaldehyde (APAL) and 3-glutamyl-3-aminopropionaldehyde (GluAPAL) ? produced in spermine (Spm), spermidine (Spd), and diaminopropane (Dap) degradation, as well as 4-aminobutyraldehyde (ABAL) and 4-glutamyl-4-aminobutyraldehyde (GluABAL) ? formed in putrescine (Put) degradation. As the catalytic efficiency of PaPauC with APAL was 30-times lower than with GluAPAL, and GluAPAL is predominantly formed, APAL will be poorly oxidized ‘in vivo’. We found polyamines-induced increases in the PaPauC activity of cell crude-extracts and in the expression of the PapauC gene that were diminished by glucose. Spm, Spd, or Dap, but not Put, were toxic to P. aeruginosa even in the presence of other carbon and nitrogen sources, particularly to a strain with the PapauC gene disrupted. APAL, but not GluAPAL, was highly toxic even to wild-type cells, suggesting that its accumulation, particularly in the absence of, or low, PaPauC activity is responsible for the toxicity of Spm, Spd, and Dap. Our results shed light on the toxicity mechanism of these three polyamines and strongly support the critical role of PaPauC in this toxicity. Thus, PaPauC emerges as a novel potential drug target whose inhibition might help in combating infection by this important pathogen.

Papain-Specific Activating Esters in Aqueous Dipeptide Synthesis

de Beer, Roseri J.A.C.,Zarzycka, Barbara,Mariman, Michiel,Amatdjais-Groenen, Helene I.V.,Mulders, Marc J.,Quaedflieg, Peter J.L.M.,van Delft, Floris L.,Nabuurs, Sander B.,Rutjes, Floris P.J.T.

experimental part, p. 1319 - 1326 (2012/08/28)

Enzymatic peptide synthesis has the potential to be a viable alternative for chemical peptide synthesis. Because of the increasing commercial interest in peptides, new and improved enzymatic synthesis methods are desirable. In recently developed enzymatic strategies such as substrate mimetic approaches and enzyme-specific activation, use of the guanidinophenyl ester (OGp) group has been shown to suffer from some drawbacks. OGp esters are sensitive to spontaneous chemical hydrolysis and the group is expensive to synthesize and therefore not suitable for large-scale applications. On the basis of earlier computational studies, we hypothesized that OGp might be replaceable by simpler ester groups to make the enzyme-specific activation approach to peptide bond formation more accessible. To this end, a set of potential activating esters (Z-Gly-Act) was designed, synthesized, and evaluated. Both the benzyl (OBn) and the dimethylaminophenyl (ODmap) esters gave promising results. For these esters, the scope of a model dipeptide synthesis reaction under aqueous conditions was investigated by varying the amino acid donor. The results were compared with those obtained from a previous study of Z-XAA-OGp esters. Computational docking analysis of the set of esters was performed in order to provide insight into the differences in the reactivities of all the potential activating esters. Finally, selected ODmap- and OBn-activated amino acids were applied in the synthesis of two biologically active dipeptides on preparative scales.

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