16677-29-5

Usage

Uses

Used in Biochemistry Research:
Z-TYR(BZL)-OH is used as a research compound for studying the properties and interactions of amino acids and peptides. Its unique structure allows scientists to investigate the effects of the benzyloxycarbonyl and benzyl ester groups on the behavior of tyrosine in various biochemical reactions.
Used in Peptide Synthesis:
In the field of peptide synthesis, Z-TYR(BZL)-OH is used as a protected amino acid derivative. The protection of the amino and carboxyl groups by the benzyloxycarbonyl and benzyl ester groups, respectively, prevents unwanted side reactions during the synthesis process. This protection is crucial for the successful assembly of complex peptide sequences.
Used in Pharmaceutical Development:
Z-TYR(BZL)-OH is employed as a building block in the development of new pharmaceutical compounds. Its role in peptide synthesis makes it a valuable tool for creating potential drug candidates with specific biological activities, such as enzyme inhibition or receptor binding.
Used in Academic Education:
In academic settings, Z-TYR(BZL)-OH is used as a teaching aid to help students understand the principles of amino acid chemistry, peptide synthesis, and the role of protecting groups in organic synthesis. It serves as a practical example of how chemical modifications can influence the properties and reactivity of biological molecules.

Upstream product

• 16652-64-5 O-benzyl-S-tyrosine 
• 501-53-1 benzyl chloroformate 
• 315203-50-0 N-benzyloxycarbonyl-O-benzyl-L-tyrosine benzyl ester 
• 100-39-0 benzyl bromide 
• 60-18-4 L-tyrosine 
• 1164-16-5 Z-L-Tyr-OH 

Downstream Products

• 3562-03-6 Z-Tyr(OBzl)-ONp 
• 106629-52-1 N,N'-Bis-(O-benzyl-N-benzyloxycarbonyl-L-tyrosyl)-ethylendiamin 
• 85512-54-5 Z-Tyr(Bzl)-piperidide 
• 52773-66-7 benzyloxycarbonyl-O-benzyl-L-tyrosine 1-succinimidyl ester 
• 90427-46-6 Z-Tyr(OBzl)-ONB 
• 75243-87-7 (S)-2-Benzyloxycarbonylamino-3-(4-benzyloxy-phenyl)-propionic acid 3-oxo-2-phenyl-3H-inden-1-yl ester 
• 81638-97-3 O-(N-benzyloxycarbonyl-O-benzyl-L-tyrosyl)-2-pyridylmethylketoxime 
• 16677-35-3 N-benzyloxycarbonyl-O-benzyl-(S)tyrosyl-glycine methyl ester 
• 108379-23-3 Z-Tyr(Bzl)-OTAP 
• 74802-24-7 benzyloxycarbonyl-O-benzyl-L-tyrosylglycylglycine p-nitrophenyl ester 
• 113266-50-5 {2-[(S)-2-Benzyloxycarbonylamino-3-(4-benzyloxy-phenyl)-propionylamino]-thioacetylamino}-acetic acid phenyl ester 
• 113266-48-1 (S)-2-[(S)-2-(2-{2-[(S)-2-Benzyloxycarbonylamino-3-(4-benzyloxy-phenyl)-propionylamino]-thioacetylamino}-acetylamino)-3-phenyl-propionylamino]-4-methyl-pentanoic acid methyl ester 
• 80633-18-7 Z-Tyr-(OBzl)-ONp-Pic 
• 73994-86-2 benzyloxycarbonyl-O-benzyl-L-tyrosyl-2-methylalanine p-nitrophenyl ester 

Relevant academic research and scientific papers

LAT1 activity of carboxylic acid bioisosteres: Evaluation of hydroxamic acids as substrates

Large neutral amino acid transporter 1 (LAT1) is a solute carrier protein located primarily in the blood–brain barrier (BBB) that offers the potential to deliver drugs to the brain. It is also up-regulated in cancer cells, as part of a tumor's increased metabolic demands. Previously, amino acid prodrugs have been shown to be transported by LAT1. Carboxylic acid bioisosteres may afford prodrugs with an altered physicochemical and pharmacokinetic profile than those derived from natural amino acids, allowing for higher brain or tumor levels of drug and/or lower toxicity. The effect of replacing phenylalanine's carboxylic acid with a tetrazole, acylsulfonamide and hydroxamic acid (HA) bioisostere was examined. Compounds were tested for their ability to be LAT1 substrates using both cis-inhibition and trans-stimulation cell assays. As HA-Phe demonstrated weak substrate activity, its structure–activity relationship (SAR) was further explored by synthesis and testing of HA derivatives of other LAT1 amino acid substrates (i.e., Tyr, Leu, Ile, and Met). The potential for a false positive in the trans-stimulation assay caused by parent amino acid was evaluated by conducting compound stability experiments for both HA-Leu and the corresponding methyl ester derivative. We concluded that HA's are transported by LAT1. In addition, our results lend support to a recent account that amino acid esters are LAT1 substrates, and that hydrogen bonding may be as important as charge for interaction with the transporter binding site.

Synthesis of enantiopure free and N-benzyloxycarbonyl-protected 3-substituted homotaurines from naturally occurring amino acids

Enantiopure N-benzyloxycarbonyl-protected and free 3-substituted homotaurines were synthesized from naturally occurring amino acids via N-benzyloxycarbonyl protection, Arndt-Eistert homologation, reduction, esterification with thioacetic acid, and oxidation with performic acid. The current method is a convenient, practical, and salt-free method for the synthesis of enantiopure 3-substituted homotaurine with moderate to good yields.

Synthesis of enantiopure free and N-benzyloxycarbonyl-protected 3-substituted homotaurines from naturally occurring amino acids

Enantiopure N-benzyloxycarbonyl-protected and free 3-substituted homotaurines were synthesized from naturally occurring amino acids via N-benzyloxycarbonyl protection, Arndt-Eistert homologation, reduction, esterification with thioacetic acid, and oxidation with performic acid. The current method is a convenient, practical, and salt-free method for the synthesis of enantiopure 3-substituted homotaurine with moderate to good yields.

Pd/C(en)-catalyzed chemoselective hydrogenation with retention of the N-Cbz protective group and its scope and limitations

A chemoselective method for the hydrogenation of acetylene, olefin, azide, nitro and benzyl ester functionalities with retention of the aliphatic N-Cbz group was established. The chemoselectivity was accomplished by using a combination of 5% Pd/C-ethylenediamine [5% Pd/C(en)] and THF (or 1,4-dioxane) as a solvent, and the scope and limitations of this methodology were investigated. These results reinforce the utility of N-Cbz protective groups in synthetic chemistry, especially in peptide synthesis. (C) 2000 Elsevier Science Ltd.