26400-33-9 Usage
Description
FA-GLY-LEU-NH2, also known as a peptide substrate, is a compound consisting of the amino acids phenylalanine (FA), glycine (GLY), leucine (LEU), and an amino group (NH2). It is designed to interact with proteinase-inhibiting proteins, which are essential for regulating the activity of proteinases, enzymes that break down proteins.
Uses
Used in Pharmaceutical Applications:
FA-GLY-LEU-NH2 is used as a substrate for natural or recombinant proteinase-inhibiting proteins to suppress proteinase activity. This interaction is crucial for maintaining the balance between protein synthesis and degradation, which is essential for various biological processes and preventing diseases related to uncontrolled protein degradation.
Used in Research and Development:
In the field of research, FA-GLY-LEU-NH2 is used as a tool to study the mechanisms of proteinase inhibition and to develop new therapeutic strategies targeting proteinases. By understanding how this peptide substrate interacts with proteinase-inhibiting proteins, researchers can gain insights into the development of novel drugs and therapies for various diseases, including those involving abnormal protein degradation.
Used in Drug Delivery Systems:
Similar to gallotannin, FA-GLY-LEU-NH2 can also be incorporated into drug delivery systems to improve its bioavailability and therapeutic outcomes. By using various organic and metallic nanoparticles as carriers, the delivery, efficacy, and targeting of FA-GLY-LEU-NH2 to specific cells or tissues can be enhanced, potentially leading to more effective treatments for diseases associated with proteinase dysregulation.
Used in Diagnostic Applications:
FA-GLY-LEU-NH2 can be employed in the development of diagnostic tools to detect and monitor proteinase activity. By measuring the interaction between this peptide substrate and proteinase-inhibiting proteins, researchers and clinicians can assess the status of proteinase regulation in a patient, which may provide valuable information for diagnosing and managing diseases related to protein degradation.
Check Digit Verification of cas no
The CAS Registry Mumber 26400-33-9 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,6,4,0 and 0 respectively; the second part has 2 digits, 3 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 26400-33:
(7*2)+(6*6)+(5*4)+(4*0)+(3*0)+(2*3)+(1*3)=79
79 % 10 = 9
So 26400-33-9 is a valid CAS Registry Number.
InChI:InChI=1/C15H21N3O4/c1-10(2)8-12(15(16)21)18-14(20)9-17-13(19)6-5-11-4-3-7-22-11/h3-7,10,12H,8-9H2,1-2H3,(H2,16,21)(H,17,19)(H,18,20)
26400-33-9Relevant articles and documents
Protease-Catalyzed Peptide Formation under High Pressure
Kunugi, Shigeru,Tanabe, Kazuo,Yamashita, Kouji,Morikawa, Yoshio,Ito, Takanobu,et al.
, p. 514 - 518 (2007/10/02)
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.
