83871-06-1

Basic information

• Product Name: Z-PHE-PRO-NH2
• Synonyms: Z-PHENYLALANINE-L-PROLINE AMIDE;Z-PHE-PRO-NH2
• CAS NO: 83871-06-1
• Molecular Formula: C₂₂H₂₅N₃O₄
• Molecular Weight: 395.45
• Mol File: 83871-06-1.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: Z-PHE-PRO-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: Z-PHE-PRO-NH2(83871-06-1)
• EPA Substance Registry System: Z-PHE-PRO-NH2(83871-06-1)

Safety Data

• Hazardous Substances Data: 83871-06-1(Hazardous Substances Data)

Upstream product

• 7669-64-9 (2S)-1-((2S)-2-[[(benzyloxy)carbonyl]amino]-3-phenylpropanoyl)tetrahydro-1H-pyrrole-2-carboxylic acid 
• 126028-14-6 2,2,2-trifluoroethyl ((benzyloxy)carbonyl)-L-phenylalaninate 
• 7531-52-4 L-prolinamide 
• 35909-92-3 N-carbobenzoxy-L-phenylalanine methyl ester 
• 4816-89-1 Cbz-Phe-OCH₂CONH₂ 
• 1161-13-3 N-Cbz-L-Phe 
• 5491-18-9 (S)-N-(benzyloxycarbonyl)phenylglycine 
• 71989-31-6 Fmoc-Pro-OH 
• 42429-27-6 L-prolinamide hydrochloride 

Downstream Products

• 81500-70-1 4-chloroacetylbenzoyl-L-Phe-L-Pro-NH₂ 
• 81500-69-8 3-chloroacetylbenzoyl-L-Phe-L-Pro-NH₂ 
• 66759-53-3 cyclo (L-Phe-L-Pro) 
• 83871-05-0 phenylalanylproline amide hydrochloride 

Relevant articles and documents

A convenient method for the one-step synthesis of phosphonic peptides

A novel and efficient method for the synthesis of peptidyl derivatives of 1-aminoalkylphosphonate diaryl esters is presented. Phosphonic peptides were obtained in one step via an amidoalkylation reaction using amides of N-protected amino acids or peptides, triphenyl phosphite, and an appropriate aldehyde.

Enzymatic synthesis of activated esters and their subsequent use in enzyme-based peptide synthesis

Chemoenzymatic peptide synthesis is potentially the most cost-efficient technology for the synthesis of short and medium-sized peptides. However, there are still some limitations when challenging peptides, e.g. containing sterically demanding acyl donors, non-proteinogenic amino acids or proline residues, are to be synthesized. To remedy these limitations, special ester moieties have been used that are specifically recognized by the enzyme, e.g. guanidinophenyl, carboxamidomethyl (Cam) or trifluoroethyl (Tfe) esters, which, unfortunately, are notoriously difficult to synthesize chemically. Herein, we demonstrate that Cam and Tfe esters are very useful for Alcalase-CLEA mediated peptide synthesis using sterically demanding and non-proteinogenic acyl donors as well as poor nucleophiles, and combinations thereof. Furthermore, these esters can be efficiently synthesized by using the lipase Cal-B or Alcalase-CLEA. Finally, it is shown that the ester synthesis by Cal-B and subsequent peptide synthesis by Alcalase-CLEA can be performed simultaneously using a two-enzyme-one-pot approach with glycolamide or 2,2,2-trifluoroethanol as additive.

PyOxP and PyOxB: The Oxyma-based novel family of phosphonium salts

Recent studies described the great impact of a non-benzotriazolic family of coupling reagents based on ethyl 2-cyano-2-(hydroxyimino)acetate, Oxyma, as a powerful coupling methodology for peptide synthesis. Here we present the synthesis and evaluation of the derived phosphonium salts O-[(1-cyano-2-ethoxy- 2-oxoethylidene)amino]-oxytri(pyrrolidin-1-yl) phosphonium hexafluorophosphate (PyOxP) and tetrafluoroborate (PyOxB). Both coupling reagents exhibited higher capacity to suppress racemization in various peptide models and enhanced solubility in DMF and DCM than benzotriazole-based reagents. In addition, the hexafluorophosphate analog PyOxP, combined excellent stability with outstanding efficiency in the assembly of demanding penta and decapeptides that include consecutive Aib residues. Cyclization models revealed the advantages of PyOxP, which rendered a higher percentage of cyclic material than other known potent phosphonium salts.

Peptide coupling in the presence of highly hindered tertiary amines

Previously, 2,4,6-trimethylpyridine (collidine), due to steric shielding around the N-atom, was found to be an efficient base for effecting peptide segment coupling via azabenzotriazole-based onium-style coupling reagents. A number of even more highly hin

Potential thyroliberin affinity labels. II: Chloroacetyl substituted phenylalanyl prolineamides

Three analogs of thyroliberin (I) were prepared. These compounds, N-m-chloroacetylbenzoyl-phenylalanyl-prolineamide (VIa), N-p-chloroacetylbenzoyl-phenylalanyl-prolineamide (VIb) and N-chloroacetyl-alanyl-phenylalanyl-prolineamide (IX), were designed as potential I antagonist affinity labels. However, no significant antagonist activity was observed. Compounds VIa and IX were found to have weak agonist activity. Cyclo (Phe-Pro) an analog of the I metabolite, cyclo (His-Pro), was found, however, to have significant I antagonist activity, but no agonist activity.