83661-95-4

Usage

Uses

Used in Pharmaceutical Industry:
FA-PHE-PHE-OH is used as a building block for the synthesis of peptides and peptide-based drugs, contributing to the development of novel pharmaceuticals targeting a variety of diseases and conditions, including cancer and neurological disorders.
Used in Medicinal Chemistry Research:
FA-PHE-PHE-OH is used as a valuable tool for studying peptide stability, transport, and metabolism in the body, aiding researchers in understanding the behavior of peptides and their potential therapeutic applications.

Upstream product

• 26390-02-3 N-<3-(2-furyl)acryloyl>-Phe-Phe-NH2 
• 5241-58-7 L-Phenylalanine amide 
• 3182-93-2 (L)-phenylalanine ethyl ester hydrochloride 
• 65864-22-4 (S)-2-amino-3-phenylpropionamide hydrochloride 
• 63-91-2 L-phenylalanine 
• 71067-15-7 C₂₀H₁₈N₂O₆ 
• 71115-83-8 N-<3-(2-furyl)acryloyl>-Phe 

Relevant academic research and scientific papers

Characterization of the substrate specificity of human carboxypeptidase A4 and implications for a role in extracellular peptide processing

CPA4 (carboxypeptidase A4) is a member of the metallocarboxypeptidase family. CPA4 was originally found in a screen of mRNAs up-regulated by sodium butyrate-induced differentiation of cancer cells. Further studies suggested a relation between CPA4 and prostate cancer aggressiveness. In the present study, we determined that CPA4 is secreted from cells as a soluble proenzyme (pro-CPA4) that can be activated by endoproteases, such as trypsin. Three complementary approaches were used to study the substrate specificity of CPA4; kinetic analysis was performed using a new series of chromogenic substrates and some biologically relevant peptides, the cleavage of synthetic peptides was tested individually, and the cleavage of a mixture of >100 mouse brain peptides was examined using a quantitative peptidomics mass spectrometry-based approach. CPA4 was able to cleave hydrophobic C-terminal residues with a preference for Phe, Leu, Ile, Met, Tyr, and Val. However, not all peptides with C-terminal hydrophobic residues were cleaved, indicating the importance of additional residues within the peptide. Aliphatic, aromatic, and basic residues in the P1 position have a positive influence on the cleavage specificity. In contrast, acidic residues, Pro, and Gly have a negative influence in the P1 position. Some of the peptides identified as CPA4 substrates (such as neurotensin, granins, and opioid peptides) have been previously shown to function in cell proliferation and differentiation, potentially explaining the link between CPA4 and cancer aggressiveness. Taken together, these studies suggest that CPA4 functions in neuropeptide processing and regulation in the extracellular environment.

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.

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.

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.

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.