16881-42-8

Basic information

• Product Name: Z-GLN-OTBU
• Synonyms: N-ALPHA-CARBOBENZOXY-L-GLUTAMINE T-BUTYL ESTER;Z-GLN-OTBU;Z-L-GLUTAMINE T-BUTYL ESTER;N2-benzyl tert-butyl N2-carboxy-L-(2-aminoglutaramate;N-.ALPHA.-Z -L-GLUTAMINE .ALPHA.-TERT.BUTYL ESTER;N2-Phenylmethoxycarbonyl-L-glutamine 1,1-dimethylethyl ester;Einecs 240-912-8;CBZ-Gln-OtBu
• CAS NO: 16881-42-8
• Molecular Formula: C₁₇H₂₄N₂O₅
• Molecular Weight: 336.38
• EINECS: 240-912-8
• Mol File: 16881-42-8.mol

Chemical Properties

• Melting Point: 94-95 °C
• Boiling Point: 549.9°Cat760mmHg
• Flash Point: 286.4°C
• Appearance: /
• Density: 1.168g/cm³
• Vapor Pressure: 3.85E-12mmHg at 25°C
• Refractive Index: 1.524
• Storage Temp.: 2-8°C
• PKA: 10.83±0.46(Predicted)
• CAS DataBase Reference: Z-GLN-OTBU(CAS DataBase Reference)
• NIST Chemistry Reference: Z-GLN-OTBU(16881-42-8)
• EPA Substance Registry System: Z-GLN-OTBU(16881-42-8)

Safety Data

• Hazardous Substances Data: 16881-42-8(Hazardous Substances Data)

Usage

Uses

Used in Organic Synthesis:
Z-GLN-OTBU is used as a building block for the synthesis of complex organic molecules. Its protecting groups allow for selective reactions, which is crucial for the successful assembly of intricate molecular structures.
Used in Peptide Chemistry:
In peptide chemistry, Z-GLN-OTBU is used as a protected amino acid for the stepwise assembly of peptides. The Z-protecting group ensures that the amine group of glutamine does not react prematurely during the peptide synthesis process, while the OTBU group protects the carboxylic acid group, maintaining the integrity of the molecule until deprotection is required.
Used in Biochemistry Research:
Z-GLN-OTBU is utilized in biochemical research for the study of peptide and protein synthesis, modification, and function. Its selective protection allows researchers to investigate the roles of specific amino acids within biologically active molecules and to develop new methods for protein engineering.
Used in Pharmaceutical Development:
In the pharmaceutical industry, Z-GLN-OTBU is used for the development of peptide-based drugs. Its ability to protect specific functional groups during synthesis enables the production of therapeutic peptides with precise sequences and structures, potentially leading to more effective medications.
Used in Chemical Education:
Z-GLN-OTBU serves as an educational tool in teaching the principles of organic synthesis, peptide chemistry, and the use of protecting groups. It provides a practical example for students to understand the importance of selective reactions and the role of protecting groups in the synthesis of complex molecules.

InChI:InChI=1/C17H24N2O5/c1-17(2,3)24-15(21)13(9-10-14(18)20)19-16(22)23-11-12-7-5-4-6-8-12/h4-8,13H,9-11H2,1-3H3,(H2,18,20)(H,19,22)

Upstream product

• 2650-64-8 Cbz-L-Gln 
• 115-11-7 isobutene 
• 507-19-7 t-butyl bromide 
• 501-53-1 benzyl chloroformate 
• 56-85-9 L-glutamine 
• 540-88-5 acetic acid tert-butyl ester 

Downstream Products

• 32908-83-1 (S)-2-((S)-2-Benzyloxycarbonylamino-4-methyl-pentanoylamino)-4-carbamoyl-butyric acid tert-butyl ester 
• 5132-46-7 H-Gln-O-Bu^t 
• 1027166-78-4 4-amino-2-benzyloxycarbonylamino-butyric acid tert-butyl ester 
• 95064-03-2 (S)-4-Carbamoyl-2-(4-methylamino-benzoylamino)-butyric acid tert-butyl ester 
• 95063-91-5 (S)-4-Carbamoyl-2-{4-[methyl-(2,2,2-trifluoro-acetyl)-amino]-benzoylamino}-butyric acid tert-butyl ester 
• 95064-05-4 (S)-2-{4-[(5-Amino-6-cyano-pyrazin-2-ylmethyl)-methyl-amino]-benzoylamino}-4-carbamoyl-butyric acid tert-butyl ester 
• 95064-04-3 N--L-glutamine t-butyl ester 

Relevant articles and documents

Preparation method of Nalpha-fluorenylmethoxycarbonyl-glutamine tert-butyl ester

The invention discloses a preparation method of Nalpha-fluorenylmethoxycarbonyl-glutamine tert-butyl ester and mainly solves the technical problems of complexity, long period, low yield, high cost and the like of an original technology. The preparation method comprises steps as follows: step one, gln and tert-butyl acetate are mixed, and h-gln-otbu is prepared under the action of perchloric acid; or, gln and z-cl are mixed, z-gln-oh is prepared and mixed with tert-butyl acetate, z-gln-otbu is prepared and subjected to catalytic hydrogenation in methyl alcohol, and h-gln-otbu is prepared; step two, h-gln-otbu and a fmoc-group protective agent are mixed, pH value is regulated to 8-9 by an alkali compound sodium carbonate aqueous solution in the presence of an organic solvent, fmoc-gln-otbu is prepared through reaction, and a pure product of fmoc-gln-otbu is prepared through processing. With the adoption of setting of a reasonable process route, Nalpha-fluorenylmethoxycarbonyl-glutamine tert-butyl ester and an intermediate thereof are prepared, and Nalpha-fluorenylmethoxycarbonyl-glutamine tert-butyl ester is applicable to mass production.

Synthesis and evaluation of peptidomimetics as selective inhibitors and active site probes of nitric oxide synthases

Nitric oxide synthase (NOS) catalyzes the conversion of L-arginine to L- citrilline and nitric oxide (NO). Selective inhibition of the isoforms of NOS could have great therapeutic potential in the treatment of certain disease states arising from pathologically elevated synthesis of NO. Recently, we reported dipeptide amides containing a basic amine side chain as potent and selective inhibitors of neuronal NOS (Huang, H.; Martasek, P.; Roman, L. J.; Masters, B. S. S.; Silverman, R. B. J. Med. Chem. 1999, 42, 3147). The most potent nNOS inhibitor among these compounds is L-Arg(NO2)-L-Dbu-NH2 (1) (K(i) = 130 nM), which also exhibits the highest selectivity over eNOS (>1500-fold) with excellent selectivity over iNOS (190-fold). Here we describe the design and synthesis of a series of peptidomimetic analogues of this dipeptide as potential selective inhibitors of nNOS. The biochemical evaluation of these compounds also revealed the binding requirements of the dipeptide inhibitors with NOS. Incorporation of protecting groups at the N- terminus of the dipeptide amide 1 (compounds 4 and 5) resulted in dramatic decreases in the inhibitory potency of nNOS. Masking the NH group of the peptide bond (peptoids 6-8 and N-methylated compounds 9-11) also gave much poorer nNOS inhibitors than 1. Both of the results demonstrate the importance of the α-amine of the dipeptide and the NH moiety of the peptide bond for binding at the active site. Modifications at the C-terminus of the peptide included converting the amide to the methyl ester (12), tert-butyl ester (13), and carboxylic acid (14) and also descarboxamide analogues (15-17), which revealed less restricted binding requirements for the C-terminus of the dipeptide. Further optimization should be possible when we learn more about the binding requirements at the active sites of NOSs.

Facile synthesis of tert-butyl ester of N-protected amino acids with tert-butyl bromide

A facile synthesis of a wide variety of N-benzyloxycarbonyl-amino acid-tert-butyl ester derivatives under mild conditions is described. N-protected amino acids were esterified with tert-butyl bromide in dimethylacetamide as solvent, in the presence of benzyltriethylammonium chloride (BTEAC)and a large excess of potassium carbonate. Many amino Z-acid-Tert-butyl esters that might be difficult to prepare by other methods have been synthesized in high yields by this procedure. The reaction is simple, unexpansive, easily scaled up, and proceeds without observable racemization.

Synthesis of Monoamides of Methotrexate from L-Glutamic Acid Monoamide t-Butyl Esters

Analoques of methotrexate (amethopterin) (1) with α- or γ-monoamide functions were synthesized starting with t-butyl L-isoglutamine (12a), t-butyl L-glutamine (22a), or the appropriate N'-alkyl or N'N'-dialkyl analoques (12b-k), (22d), (22k), (22l), and (22m).The corresponding N-benzyloxycarbonyl compounds (11) and/or (21) from which the above L-glutamic acid derivatives were obtained were generally synthesized by mixed-anhydride coupling of N-benzyloxycarbonyl-L-glutamic acid (9) with the appropriate amine, conversion into the t-butyl ester, and chromatographic separation.The resulting α-monoamide γ-t-butyl ester (11) and γ-monoamide α-t-butyl ester (21) are unambiguously distinguished by mass spectrometry and 13C n.m.r. spectroscopy.Factors which affect the γ-amide/α-amide product ratio are discussed.The N-deprotected L-glutamic acid monoamide t-butyl esters (12) or (22) were individually coupled to N-trifluoroacetyl-p-methylaminobenzoic acid, and the resulting α- or γ-monoamide t-butyl esters (13) or (23) of N-(p-methyl(trifluoroacetyl)aminobenzoyl)-L-glutamic acid was hydrolysed.The N-deprotected product, viz. t-butyl N-(p-methylaminobenzoyl)-L-glutamate α- or γ-monoamide (14) or (24) was converted into the appropriate methotrexate-monoamide t-butyl ester (15) or (25), and thence the desired methotrexate-monoamide (16) or (26), by reaction with 2,4-diamino-6-bromomethylpteridine (17) or by the Taylor procedure.Features of the mass and 13C n.m.r. spectra of the intermediates are discussed.