61430-17-9 Usage
Uses
Used in Pharmaceutical Industry:
H-ALA-ALA-PRO-ALA-ALA-OH is used as a potential drug candidate for its antimicrobial, antiviral, and anticancer properties. Its unique chemical structure allows it to target various biological pathways and mechanisms, making it a promising option for the development of new therapeutic agents.
Used in Drug Design and Development:
H-ALA-ALA-PRO-ALA-ALA-OH is utilized as a building block in the design and development of new drugs. Its specific amino acid composition and sequence contribute to its biological activities, which can be harnessed to create effective treatments for various diseases and conditions.
Used in Antimicrobial Applications:
H-ALA-ALA-PRO-ALA-ALA-OH is employed as an antimicrobial agent, targeting and inhibiting the growth of harmful microorganisms. Its peptide structure allows it to interact with bacterial cell walls and membranes, disrupting their function and leading to their destruction.
Used in Antiviral Applications:
H-ALA-ALA-PRO-ALA-ALA-OH is used as an antiviral agent, capable of inhibiting the replication and spread of viruses. Its peptide nature enables it to interfere with viral entry, assembly, or release, thereby reducing viral load and limiting the severity of infections.
Used in Anticancer Applications:
H-ALA-ALA-PRO-ALA-ALA-OH is used as an anticancer agent, targeting and disrupting the growth and proliferation of cancer cells. Its potential to modulate various oncological signaling pathways and exhibit synergistic effects with conventional chemotherapeutic drugs makes it a promising candidate for cancer treatment.
Check Digit Verification of cas no
The CAS Registry Mumber 61430-17-9 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 6,1,4,3 and 0 respectively; the second part has 2 digits, 1 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 61430-17:
(7*6)+(6*1)+(5*4)+(4*3)+(3*0)+(2*1)+(1*7)=89
89 % 10 = 9
So 61430-17-9 is a valid CAS Registry Number.
61430-17-9Relevant academic research and scientific papers
Investigations of the mechanism of the proline effect in tandem mass spectrometry experiments: The pipecolic acid effect
Raulfs, Mary Disa M.,Breci, Linda,Bernier, Matthew,Hamdy, Omar M.,Janiga, Ashley,Wysocki, Vicki,Poutsma, John C.
, p. 1705 - 1715 (2015/02/19)
The fragmentation behavior of a set of model peptides containing proline, its four-membered ring analog azetidine-2-carboxylic acid (Aze), its six-membered ring analog pipecolic acid (Pip), an acyclic secondary amine residue N-methyl-alanine (NMeA), and the D stereoisomers of Pro and Pip has been determined using collision-induced dissociation in ESI-tandem mass spectrometers. Experimental results for AAXAA, AVXLG, AAAXA, AGXGA, and AXPAA peptides are presented, where X represents Pro, Aze, Pip, or NMeA. Aze- and Pro-containing peptides fragment according to the well-established proline effect through selective cleavage of the amide bond N-terminal to the Aze/Pro residue to give yn + ions. In contrast, Pip- and NMA-fragment through a different mechanism, the pipecolic acid effect, selectively at the amide bond C-terminal to the Pip/NMA residue to give bn + ions. Calculations of the relative basicities of various sites in model peptide molecules containing Aze, Pro, Pip, or NMeA indicate that whereas the proline effect' can in part be rationalized by the increased basicity of the prolyl-amide site, the pipecolic acid effect cannot be justified through the basicity of the residue. Rather, the increased flexibility of the Pip and NMeA residues allow for conformations of the peptide for which transfer of the mobile proton to the amide site C-terminal to the Pip/NMeA becomes energetically favorable. This argument is supported by the differing results obtained for AAPAA versus AA(D-Pro)AA, a result that can best be explained by steric effects. Fragmentation of pentapeptides containing both Pro and Pip indicate that the pipecolic acid effect is stronger than the proline effect.
