71115-83-8

Usage

Uses

Used in Pharmaceutical Industry:
FA-PHE-OH is used as a detection agent for angiotensin-converting enzyme (ACE) inhibitors. It is particularly useful in the development and testing of new drugs that target ACE, which plays a crucial role in regulating blood pressure and is a common target for hypertension treatments. By using FA-PHE-OH on 96 well plates, researchers can efficiently screen and identify potential ACE inhibitors, accelerating the drug discovery process.

Upstream product

• 598-41-4 H-Gly-NH₂ 
• 90846-39-2 N-<3-(2-furyl)acryloyl>-Phe-Gly-NH2 
• 1668-10-6 glycinamide hydrochloride 
• 65376-39-8 N-[3-(2-furyl)acryloyl]-phenylalanine methyl ester 
• 20689-54-7 3-furanylacryloyl chloride 
• 539-47-9 3-(2-furyl)acrylic acid 
• 5241-58-7 L-Phenylalanine amide 
• 687-51-4 H-L-Leu-NH₂ 
• 26390-02-3 N-<3-(2-furyl)acryloyl>-Phe-Phe-NH2 
• 65864-22-4 (S)-2-amino-3-phenylpropionamide hydrochloride 

Downstream Products

• 83661-95-4 3-(2-furyl)acryloylglycyl-L-phenylalanine-L-phenylalanine 
• 1236954-99-6 FA-Phe-His 
• 93936-28-8 FA-Phe-Val 
• 1236954-97-4 FA-Phe-Met 
• 1236954-94-1 FA-Phe-Ile 
• 1236954-92-9 C₂₇H₂₅N₃O₅ 
• 71067-15-7 C₂₀H₁₈N₂O₆ 

Relevant academic research and scientific papers

The Effect of Pressure on Protease-catalysed Peptide Formation

Peptide formation from an N-acyl amino acid ester and an amino acid amide using carboxypeptidase Y as a catalyst was shown to be considerably influenced by applying high pressure; at 150 MPa the peptide yield was almost five-fold higher than that at 0.1 MPa when PheNH2 was used as the nucleophile.

Wheat Carboxypeptidase-Catalyzed Peptide Synthesis by Aminolysis of N-Acyl Amino Acid Ester. Indication of the Acyl-Enzyme Mechanism

Dipeptide synthesis from N--acylated (Fua-) amino acid ethyl ester and amino acid amide catalyzed by wheat bran carboxypeptidase (carboxypeptidase W) was studied.The optimum pH for peptide formation was at pH 8; more than 60 percent of the initial N-Fua-L-phenylalanine ethyl ester was converted to N-Fua-L-phenylalnylglycinamide under optimum conditions.The dependence of peptide formation on the concentration of amino acid amide showed an apparent saturation; this could be successfully explained by a reaction scheme which involved an acylated enzyme attacked by an enzyme-bound amine.The results for a reaction in the presence of two different amine components also supported this mechanism.Gly-NH2 had a better affinity to the acylated carboxypeptidase and the apparent dissociation constants (KN(app)) was about 50 mM.These results were compared with those for those reactions catalyzed by carboxypeptidases from yeast and malt.

Synthesis of some amino acid and peptide conjugates and their evaluation as potential anti-allergic and anti-inflammatory agents

ANEW series of N-3-(2-furanyl) acryloyl, N-3-(5-methyl)-2-(furanyl)-acryoyl amino acids, peptide and piprazines amids, were structurally designed and synthesized. About 23 compounds (5a-w) were synthesized and their anti-allergic and anti-inflamatory acti

Protease-Catalyzed Peptide Formation under High Pressure

The effect of high pressure on peptide formation by the catalysis of carboxypeptidase Y (substitution of ester or peptide by amino acid derivative) or by thermolysin (condensation of N-acylamino acid and amino acid amide) was studied.The carboxypeptidase Y-catalyzed substitution reaction of N-phenylalanine ethyl ester with glycinamide or phenylalaninamide showed a six-fold higher total peptide yield at 200 MPa than at atmospheric pressure.In the case of the reaction of N-acyldipeptide and amino acid amide, both the peptide yield and substitution efficiency were improved at elevated pressure and the wasteful hydrolysis of the substrate was highly depressed by increasing pressure.The pressure was also effective to get rid of the substrate inhibition by the amino acid ester inthe reaction between the N-acylamino acid ester and the amino acid ester and to yield much dipeptide ester at high pressure.An improvement of the peptide yield by pressure for the reaction of thermolysin was observed in a combination of less specific substrates, N-benzyloxycarbonyl-L-aspartic acid and phenylalanine methyl ester, since the high catalytic activity of this enzyme under elevated pressure was significant only in the case that the peptide yield was kinetic-controlled.

Action of Serine Carboxypeptidases on Endopeptidase Substrates, N-Acyldipeptideamides

Action patterns of two serine carboxypeptidases, one from yeast (Y) and the other from wheat bran (W), on N--(Fua-)-dipeptideamide substrates were examined by HPLC and amino acid analysis.In the reaction of the wheat enzyme the substrates were hydrolyzed to Fua-amino acid and no sufficient amount of Fua-dipeptides were detected on HPLC in the product mixtures.Very few or no free amino acids were observed by amino acid analysis.This indicates that the wheat enzyme exhibited carboxamidopeptidase activity on these substrates.On the contrary, carboxypeptidase Y gave Fua-amino acids and Fua-dipeptides as products, depending on the structure of the substrates.Accordingly, liberations of free amino acids were detected in some cases.This result shows that the yeast enzyme acts on some of the substrates in a two step manner: First by amidase and second by a carboxypeptidase activity.Based on these results the substrate binding mechanisms of these enzymes are discussed.