60379-01-3

Basic information

• Product Name: Z-PHE-OBZL
• Synonyms: N-ALPHA-CARBOBENZOXY-L-PHENYALANINE BENZYL ESTER;Z-PHE-OBZL;Z-PHENYLALANINE-OBZL;Z-L-PHENYLALANINE BENZYL ESTER;benzyl (2S)-3-phenyl-2-(phenylmethoxycarbonylamino)propanoate
• CAS NO: 60379-01-3
• Molecular Formula: C₂₄H₂₃NO₄
• Molecular Weight: 389.44
• Mol File: 60379-01-3.mol

Chemical Properties

• Melting Point: 63-65 °C
• Boiling Point: 566.7°C at 760 mmHg
• Flash Point: 296.5°C
• Appearance: /
• Density: 1.195g/cm³
• Vapor Pressure: 7.31E-13mmHg at 25°C
• Refractive Index: 1.592
• Storage Temp.: Store at RT.
• PKA: 10.93±0.46(Predicted)
• CAS DataBase Reference: Z-PHE-OBZL(CAS DataBase Reference)
• NIST Chemistry Reference: Z-PHE-OBZL(60379-01-3)
• EPA Substance Registry System: Z-PHE-OBZL(60379-01-3)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 60379-01-3(Hazardous Substances Data)

Usage

Uses

Used in Biochemical Research:
Z-PHE-OBZL is used as a research tool for monitoring the activity of peptidase enzymes due to its fluorogenic properties, which allow for the detection and quantification of enzyme activity through the measurement of emitted fluorescence upon peptide sequence cleavage.
Used in Pharmaceutical Development:
In the pharmaceutical industry, Z-PHE-OBZL serves as a valuable compound for the development of drugs targeting peptidase enzymes. Its ability to provide a measurable fluorescent signal upon enzyme interaction aids in the assessment of drug efficacy and the optimization of lead compounds.
Used in Diagnostic Applications:
Z-PHE-OBZL is utilized as a diagnostic agent for the detection and analysis of peptidase enzyme activity in clinical samples. Its sensitivity and specificity in response to enzyme presence make it a reliable indicator for various pathological conditions associated with altered peptidase activity.
Used in Enzyme Kinetics Studies:
Z-PHE-OBZL is employed as a substrate in enzyme kinetics studies to determine the reaction rates and mechanisms of peptidase enzymes. Z-PHE-OBZL's fluorescence emission upon cleavage provides a direct and quantitative measure of enzyme activity, facilitating the elucidation of kinetic parameters and catalytic efficiency.

InChI:InChI=1/C24H23NO4/c26-23(28-17-20-12-6-2-7-13-20)22(16-19-10-4-1-5-11-19)25-24(27)29-18-21-14-8-3-9-15-21/h1-15,22H,16-18H2,(H,25,27)/t22-/m0/s1

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 100-51-6 benzyl alcohol 
• 100-39-0 benzyl bromide 
• 124-38-9 carbon dioxide 
• 63-91-2 L-phenylalanine 
• 100-44-7 benzyl chloride 
• 962-39-0 L-Phenylalanine benzyl ester 
• 501-53-1 benzyl chloroformate 
• 5491-18-9 (S)-N-(benzyloxycarbonyl)phenylglycine 
• 150-30-1 Phenylalanine 
• 16367-71-8 t-butyl (RS)-phenylalaninate 
• 1122-58-3 dmap 
• 5241-56-5 benzyl [(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]carbamate 
• 16881-34-8 N-benzyloxycarbonyl-L-phenylalanine t-butyl ester 

Downstream Products

• 33033-71-5 (S)-tert-butyl 2-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)propanoate 
• 29842-94-2 (S)-tert-butyl 2-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)-4-methylpentanoate 
• 82610-83-1 ester ethylique de l'acide (N-benzyloxycarbonyl)-L-phenylalanyl-aminomethylphosphonique 
• 141056-54-4 N-benzyloxycarbonyl-L-phenylalanyl-L-phenylalaninamide 
• 4864-80-6 benzyl (S)-(1-((2-hydroxyethyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 115329-03-8 ((S)-1-Allylcarbamoyl-2-phenyl-ethyl)-carbamic acid benzyl ester 
• 65118-54-9 N-(benzyloxycarbonyl)phenylalanyl-alanine amide 
• 15366-12-8 (S)-benzyl (1-oxo-3-phenyl-1-(phenylamino)propan-2-yl)carbamate 
• 1161-13-3 N-Cbz-L-Phe 
• 63-91-2 L-phenylalanine 
• 35909-92-3 N-carbobenzoxy-L-phenylalanine methyl ester 

Relevant articles and documents

Development of a triazinedione-based dehydrative condensing reagent containing 4-(dimethylamino)pyridine as an acyl transfer catalyst

A new triazinedione-based reagent, (N,N′-dialkyl)triazinedione-4-(dimethylamino)pyridine (ATD-DMAP) was developed for the operationally simple dehydrative condensation of carboxylic acids. This reagent comprises an ATD core and DMAP as the leaving group, which is liberated into the reaction system to accelerate acyl transfer reactions. Upon adding ATD-DMAP to a mixture of carboxylic acids and alcohols in the presence of an amine base, the corresponding esters were formed rapidly at room temperature. Moreover, dehydrative condensation between carboxylic acids and amines using ATD-DMAP proceeded in high yield.

Development of triazine-based esterifying reagents containing pyridines as a nucleophilic catalyst

We have developed new triazine-based esterifying reagents comprising pyridines that can act as a nucleophilic catalyst. 1-(4,6-Dimethoxy-1,3,5-triazin-2-yl)-3,5-lutidinium chloride (DMT-3,5-LUT) was found to exhibit a superior reactivity for the dehydrating condensation reaction between carboxylic acids and alcohols. The reaction of DMT-3,5-LUT with carboxylic acids produces intermediacy of acyloxytriazines, which is known to exhibit moderate reactivity toward alcohols, with concomitant liberation of 3,5-lutidine. The subsequent chemical transformation of the acyloxytriazines and alcohols into esters can be accelerated by the action of 3,5-lutidine as a nucleophilic catalyst. The detailed reaction mechanism revealed by a time-course analysis of the reactions is also discussed.

A practical aryl unit for azlactone dynamic kinetic resolution: Orthogonally protected products and a ligation-inspired coupling process

The first strategy for bringing about enantioselective azlactone dynamic kinetic resolution to generate orthogonally protected amino acids has been developed. In the presence of a C2-symmetric squaramide-based catalyst, benzyl alcohol reacts with novel yet readily prepared tetrachloroisopropoxycarbonyl-substituted azlactones to generate trapped phthalimide products of significant synthetic interest with excellent enantiocontrol. These materials are masked amino acids which are demonstrably orthogonally protected: cleavage of the phthalimide can be achieved in the presence of the ester and vice versa. This process could be utilized to bring about a highly stereoselective ligation-type coupling of protected serines (at stoichiometric loadings) with racemic azlactones derived from both natural and abiotic amino acids. After deprotection, a subsequent base-mediated Oa??N acyl transfer occurs to form a dipeptide.

Solventless mechanosynthesis of N-protected amino esters

Mechanochemical derivatizations of N- or C-protected amino acids were performed in a ball mill under solvent-free conditions. A vibrational ball mill was used for the preparation of N-protected α- and β-amino esters starting from the corresponding N-unmasked precursors via a carbamoylation reaction in the presence of di-tert-butyl dicarbonate (Boc2O), benzyl chloroformate (Z-Cl) or 9-fluorenylmethoxycarbonyl chloroformate (Fmoc-Cl). A planetary ball mill proved to be more suitable for the synthesis of amino esters from N-protected amino acids via a one-pot activation/esterification reaction in the presence of various dialkyl dicarbonates or chloroformates. The spot-to-spot reactions were straightforward, leading to the final products in reduced reaction times with improved yields and simplified work-up procedures.

Fully enzymatic N→C-directed peptide synthesis using C-terminal peptide α-carboxamide to ester interconversion

Chemoenzymatic peptide synthesis is potentially the most cost-efficient technology for the synthesis of short and medium-sized peptides with some important advantages. For instance, stoichiometric amounts of expensive coupling reagents are not required and racemisation does not occur rendering purification easier compared to chemical peptide synthesis. In this paper, a novel interconversion reaction of peptide C-terminal α-carboxamides into primary alkyl esters with alcalase was used to develop a fully enzymatic peptide synthesis strategy. For each elongation step a cost-efficient amino acid carboxamide building block was used followed by the interconversion of the elongated peptide carboxamide to the corresponding primary alkyl ester. These peptide esters are the starting materials for the next enzymatic peptide elongation step. Copyright

Fully enzymatic peptide synthesis using C-terminal tert-butyl ester interconversion

Chemoenzymatic peptide synthesis is potentially the most cost-efficient technology for the synthesis of short and medium-sized peptides with some important advantages. For instance, stoichiometric amounts of expensive coupling reagents are not required an

Versatile selective α-carboxylic acid esterification of N-protected amino acids and peptides by alcalase

Under continuous removal of water, the industrial protease Alcalase allows selective synthesis of α-carboxylic acid methyl, ethyl, benzyl, allyl, 2-(trimethylsilyl)ethyl, and tert-butyl esters of amino acids and peptides under mild conditions in very high

Enzymatic synthesis of C-terminal arylamides of amino acids and peptides

(Chemical Equation Presented) A mild and cost-efficient chemo-enzymatic method for the synthesis of C-terminal arylamides of amino acid and peptides is described. Using the industrial serine protease Alcalase under near-anhydrous conditions, C-terminal arylamides of N-Cbz-protected amino acids and peptides could be obtained from the corresponding C-terminal carboxylic acids, methyl (Me) or benzyl (Bn) esters, in high chemical and enantio- and diastereomeric purities. Yields ranged between 50% and 95% depending on the size of the aryl substituents and the presence of electron-withdrawing substituents. Complete α-C-terminal selectivity could be obtained even in the presence of various unprotected side-chain functionalities such as β/γ-carboxyl, hydroxyl, and guanidino groups. In addition, the use of the cysteine protease papain and the lipase Cal-B gave anilides in high yields. The chemo-enzymatic synthesis of arylamides proved to be completely free of racemization, in contrast to the state-of-the-art chemical methods.

A novel 1-tert-butoxy-2-tert-butoxycarbonyl-1,2-dihydroisoquinoline (BBDI)-catalyzed esterification of N-protected amino acids with nearly equimolar amounts of alcohols in the presence of Boc2O

A very mild, BBDI-catalyzed esterification using approximately equimolar amounts of N-protected amino acids and alcohols, in junction with Boc2O is described.

Simple and mild esterification of N-protected amino acids with nearly equimolar amounts of alcohols using 1-tert-butoxy-2-tert-butoxycarbonyl-1,2- dihydroisoquinoline

A very mild, one-step esterification using nearly equimolar amounts of N-protected amino acids and alcohols, in conjunction with 1-tert-butoxy-2-tert- butoxycarbonyl-1,2-dihydroisoquinoline (BBDI) as a novel condensing reagent is described.