31384-90-4 Usage
Uses
Used in Pharmaceutical and Medical Industries:
BZ-GLY-GLY-GLY-OH is used as a peptide derivative for its potential applications in the pharmaceutical and medical industries due to its various biological activities.
Used in Antimicrobial Applications:
BZ-GLY-GLY-GLY-OH is used as an antimicrobial agent for its ability to target and eliminate harmful microorganisms, contributing to the development of new antibiotics and antimicrobial therapies.
Used in Anticancer Applications:
BZ-GLY-GLY-GLY-OH is used as an anticancer agent for its potential to target and inhibit the growth of cancer cells, offering a novel approach to cancer treatment and therapy.
Used in Antiviral Applications:
BZ-GLY-GLY-GLY-OH is used as an antiviral agent for its potential to inhibit viral replication and infection, providing a new avenue for the development of antiviral drugs and therapies.
Used in Drug Delivery Systems:
BZ-GLY-GLY-GLY-OH is used as a component of drug delivery systems for its potential to improve the delivery, bioavailability, and therapeutic outcomes of various drugs, particularly in the treatment of cancer and infectious diseases.
Used in Synthesis of Peptide-Based Drugs:
BZ-GLY-GLY-GLY-OH is used as a building block for the synthesis of more complex peptide-based drugs, offering a versatile platform for the development of innovative pharmaceutical compounds with diverse applications.
Check Digit Verification of cas no
The CAS Registry Mumber 31384-90-4 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,1,3,8 and 4 respectively; the second part has 2 digits, 9 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 31384-90:
(7*3)+(6*1)+(5*3)+(4*8)+(3*4)+(2*9)+(1*0)=104
104 % 10 = 4
So 31384-90-4 is a valid CAS Registry Number.
InChI:InChI=1/C13H15N3O5/c17-10(15-8-12(19)20)6-14-11(18)7-16-13(21)9-4-2-1-3-5-9/h1-5H,6-8H2,(H,14,18)(H,15,17)(H,16,21)(H,19,20)
31384-90-4Relevant articles and documents
Linear energy correlations and failures in the low-energy tandem mass spectra of protonated N-benzoylated tripeptides: Tools for probing mechanisms of CAD processes
Morgan,Bursey
, p. 595 - 600 (2007/10/02)
The backbone cleavages for three series of protonated N-benzoyl tripeptide ions were studied in a hybrid tandem mass spectrometer: (i) benzoyl-Gly-Gly-Xxx, where Xxx = Gly, Ala, Val, Leu, Ile, Phe, Tyr, Met, Glu, Pro and Trp, (ii) benzoyl-Gly-Xxx-Gly, where Xxx = Gly, Ala, Leu, Phe, Tyr, Met and Trp, and (iii) benzoyl-Xxx-Gly-Gly, where Xxx = Gly, Ale, Val, Leu, Ile, Phe, Tyr, Met, Pro and Trp. C-Terminal γ-type ions and N-terminal a- and b-type ions were noted in all three cases. For benzoyl-Gly-Gly-Xxx, a linear relationship between log(γ1/b2) and the proton affinity of the C-terminal amino acid substituents was found: as the proton affinity of the C-terminal residue increases, the fraction of γ1 ion formation increases. A similar relationship was noted for the benzoyl-Xxx-Gly-Gly tripeptides between log (γ2/b1) and the proton affinity of the N-terminal amino acid substituent: as the proton affinity of the N-terminal residue increases, the fraction of b1 ion formation increases. For the series benzoyl-Gly-Xxx-Gly, these relationships did not hold true. These observations point to similar reaction pathways throughout the benzoyl-Gly-Gly-Xxx series and also similar pathways throughout the benzoyl-Xxx-Gly-Gly, but pathways that are substituent dependent for benzoyl-Gly-Xxx-Gly. The increased correlation coefficients for benzoyl-Gly-Gly-Xxx and benzoyl-Xxx-Gly-Gly when compared with the free tripeptides, suggest that fewer interfering competitive reactions exist, as fewer possibilities for internal hydrogen bonding exist in the N-benzoyl derivatives versus the free compounds.
