17460-56-9

Basic information

• Product Name: Z-D-PHE-PRO-OH
• Synonyms: Z-PHENYLALANINE-D-PROLINE;Z-D-PHE-PRO-OH;(S)-1-((R)-2-(benzyloxycarbonylamino)-3-phenylpropanoyl)pyrrolidine-2-carboxylic acid;CBZ-D-Phe-Pro-OH;N-Benzyloxycarbonyl-D-phenylalanlyproline
• CAS NO: 17460-56-9
• Molecular Formula: C₂₂H₂₄N₂O₅
• Molecular Weight: 396.44
• Mol File: 17460-56-9.mol
• Article Data: 18

Chemical Properties

• Melting Point: 132-133 °C(Solv: ethyl ether (60-29-7))
• Boiling Point: 669.586 °C at 760 mmHg
• Flash Point: 358.753 °C
• Appearance: /
• Density: 1.292 g/cm³
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 1.604
• Storage Temp.: -15°C
• PKA: 3.51±0.20(Predicted)
• CAS DataBase Reference: Z-D-PHE-PRO-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Z-D-PHE-PRO-OH(17460-56-9)
• EPA Substance Registry System: Z-D-PHE-PRO-OH(17460-56-9)

Safety Data

• Hazardous Substances Data: 17460-56-9(Hazardous Substances Data)

Usage

Uses

Used in Biochemical Research:
Z-D-PHE-PRO-OH is used as a model compound for understanding the structural and functional aspects of peptides. It aids researchers in exploring the interactions between peptides and their target molecules, which is essential for the development of new therapeutic agents.
Used in Pharmaceutical Research and Drug Development:
In the pharmaceutical industry, Z-D-PHE-PRO-OH is employed as a precursor in the synthesis of bioactive peptides and proteins. Its use in drug development facilitates the creation of novel therapeutics with specific biological activities, contributing to advancements in medicine.
Used in Peptide Synthesis:
Z-D-PHE-PRO-OH is used as a building block in the synthesis of larger peptides and proteins. Its incorporation into these macromolecules allows for the design of complex biologically active molecules with tailored properties for various applications in medicine and biotechnology.
Overall, Z-D-PHE-PRO-OH is a versatile compound with significant implications in the fields of biochemistry, pharmaceuticals, and biotechnology, serving as a valuable tool for research and development of innovative therapeutic agents.

InChI:InChI=1/C22H24N2O5/c25-20(24-13-7-12-19(24)21(26)27)18(14-16-8-3-1-4-9-16)23-22(28)29-15-17-10-5-2-6-11-17/h1-6,8-11,18-19H,7,12-15H2,(H,23,28)(H,26,27)/t18-,19+/m1/s1

Upstream product

• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 
• 147-85-3 L-proline 
• 1161-13-3 N-Cbz-L-Phe 
• 2578-84-9 N-benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester 
• 60746-24-9 Benzyloxycarbonyl-L-phenylalanin-seleno-phenylester 
• 63358-25-8 Z-D-Phe-OTCP 
• 2812-46-6 proline tert-butyl ester 
• 2448-45-5 Cbz-D-Phe 
• 870695-98-0 benzyl (1-(1H-benzo[d][1,2,3]triazol-1-yl)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 2448-45-5 N-(Benzyloxycarbonyl)-D-phenylalanine 
• 2577-48-2 methyl (2S)-pyrrolidine carboxylate 
• 41518-17-6 Z-Phe-O-COO-isoBu 
• 501-53-1 benzyl chloroformate 
• 175446-63-6 proline acid chloride 

Downstream Products

• 162990-46-7 Cbz-(R)-Phe-Pro-BoroMpg-OPinacol 
• 139222-68-7 2-(N-benzyloxycarbonyl-L-phenylalanyl-L-prolyl-L-valyl)amino-6-methylbenzoic acid 
• 161404-03-1 Z-Tyr(Bzl)-Pro-Phe-Pro-Gly-EtDA<*>Gly<*>Gly-CO-(CH2)2-COOH 
• 161404-01-9 Z-Tyr(Bzl)-Pro-Phe-Pro-Gly-EtDA<*>Gly<*>Gly-Boc 
• 161403-95-8 Z-Tyr(Bzl)-Pro-Phe-Pro-Gly-EtDA<*>Gly-Boc 
• 161404-00-8 Z-Pro-Phe-Pro-Gly-EtDA<*>Gly<*>Gly-Boc 
• 161403-93-6 Z-Phe-Pro-Gly-EtDA<*>Gly-Boc 
• 161403-99-2 [({[2-(2-{[(S)-1-((S)-2-Amino-3-phenyl-propionyl)-pyrrolidine-2-carbonyl]-amino}-acetylamino)-ethylcarbamoyl]-methyl}-carbamoyl)-methyl]-carbamic acid tert-butyl ester 
• 161403-94-7 H-Phe-Pro-Gly-EtDA<*>Gly-Boc 
• 132370-20-8 H-Tyr-Pro-Phe-Pro-Gly-EtDA<*>Gly<*>Gly-H 
• 132370-19-5 H-Tyr-Pro-Phe-Pro-Gly-EtDA<*>Gly-H 
• 184295-92-9 (2S,3R)-2-{[(S)-1-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionyl)-pyrrolidine-2-carbonyl]-amino}-3-hydroxy-butyric acid methyl ester 
• 184295-93-0 (2S,3S)-2-{[(S)-1-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionyl)-pyrrolidine-2-carbonyl]-amino}-3-hydroxy-butyric acid methyl ester 

Relevant articles and documents

MALT1 INHIBITORS AND USES THEREOF

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A benzotriazole-mediated route to protected marine-derived hetero-2,5-diketopiperazines containing proline

A procedure for the cyclization of dipeptidoyl benzotriazolides containing proline derivatives promoted by triethylamine under MW activation is introduced. The reaction is general for a variety of dipeptidoyl benzotriazolides and represents a very practical and convenient method for the preparation of Pro- or Hyp-derived 2,5-diketopiperazines (2,5-DKPs) and bis-DKPs with a disulfide linker. This method can be used for the construction of 2,5-DKP compound libraries and for the synthesis of natural products with diketopiperazine cores. This journal is

A new benzotriazole-mediated stereoflexible gateway to hetero-2,5- diketopiperazines

Open chain Cbz-L-aa1-L-Pro-Bt (Bt=benzotriazole) sequences were converted into either the corresponding trans- or cis-fused 2,5- diketopiperazines (DKPs) depending on the reaction conditions. Thermodynamic tandem cyclization/epimerization afforded selectively the corresponding trans-DKPs (69-75%). Complementarily, tandem deprotection/cyclization led to the cis-DKPs (65-72%). A representative set of proline-containing cis- and trans-DKPs has been prepared. A mechanistic investigation, based on chiral HPLC, kinetics, and computational studies enabled a rationalization of the results. Stereoflexible route to DKPs: A convenient, versatile, and flexible benzotriazole-mediated methodology for the synthesis of proline-containing hetero-2,5-diketopiperazines (DKPs) is reported. Depending on the reaction conditions, either cis- or trans-configured DKPs were obtained starting from the same inexpensive l,l-dipeptidoyl benzotriazole key intermediate (see scheme). Kinetics, chiral HPLC, and computational studies forged a background for mechanistic rationalization. Copyright

Efficient peptide coupling involving sterically hindered amino acids

(Chemical Equation Presented) Hindered amino acids have been introduced into peptide chains by coupling N-(Cbz- and Fmoc-α-aminoacyl) benzotriazoles with amino acids, wherein at least one of the components was sterically hindered, to provide compounds 3a-e, (3c +3 c′), 5a-d, (5a + 5a′), 6a-c, (6b + 6b′), 8a-c, 9a-e, 10a-d, and (10a + 10a′) in isolated yields of 41-95% with complete retention of chirality as evidenced by NMR and HPLC analysis. The benzotriazole activation methodology is a new route for the synthesis of sterically hindered peptides. (Note: compound numbers written within brackets represent diastereomeric mixtures or racemates; compound numbers without brackets represent enantiomers.)

Microwave irradiated high-speed solution synthesis of peptide acids employing Fmoc-amino acid pentafluorophenyl esters as coupling agents

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Influence of solvent viscosity on the rate of hydrolysis of dipeptides by carboxypeptidase Y

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Relationship between the hydrophobicity of dipeptides and the Michaelis-Menten constant Km of their hydrolysis by carboxypeptidase-Y and carboxypeptidase-A

The enzymatic hydrolysis of dipeptides by carboxypeptidase-Y and carboxypeptidase-A was investigated. In the enzymatic hydrolysis of the dipeptides, a good linear relationship (r = 0.997 and 0.999) was found between the Michaelis-Menten constant (Km) and the hydrophobicity of the substrates evaluated from relative elution volume in reversed-phase HPLC. The correlation suggests that the hydrophobicity of the C-terminal amino acid is a major factor in governing the stability of the enzyme-substrate complex. The difference in the slope of the linear-regression lines seems to reflect the degree of relative hydrophobicity of the binding pockets in carboxypeptidase-Y and carboxypeptidase-A.

HETEROCYCLIC THROMBIN INHIBITORS

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Total synthesis and assignment of configuration of lissoclinamide 7

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