1445137-79-0 Usage
Uses
Used in Organic Synthesis:
2-(benzyloxycarbonylamino)-2-methylhept-6-enoic acid serves as a reagent for the protection of amino groups in peptide and protein chemistry. Its benzyloxy carbonyl moiety provides a stable and easily removable protecting group, facilitating the synthesis of complex peptide sequences and improving the yield of desired products.
Used in Pharmaceutical Synthesis:
As a building block, 2-(benzyloxycarbonylamino)-2-methylhept-6-enoic acid contributes to the synthesis of complex molecules and pharmaceuticals. Its unique structure allows for the creation of novel compounds with potential therapeutic properties, expanding the scope of drug development.
Used in Medicinal Chemistry:
2-(benzyloxycarbonylamino)-2-methylhept-6-enoic acid has potential applications in the field of medicinal chemistry, where its structural features can be exploited to design and develop new drugs with improved efficacy and selectivity. Its versatility as a building block and protecting group makes it a valuable asset in the discovery and optimization of bioactive molecules.
Check Digit Verification of cas no
The CAS Registry Mumber 1445137-79-0 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,4,4,5,1,3 and 7 respectively; the second part has 2 digits, 7 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 1445137-79:
(9*1)+(8*4)+(7*4)+(6*5)+(5*1)+(4*3)+(3*7)+(2*7)+(1*9)=160
160 % 10 = 0
So 1445137-79-0 is a valid CAS Registry Number.
1445137-79-0Relevant academic research and scientific papers
Design of cell-permeable stapled peptides as HIV-1 integrase inhibitors
Long, Ya-Qiu,Huang, Shao-Xu,Zawahir, Zahrah,Xu, Zhong-Liang,Li, Huiyuan,Sanchez, Tino W.,Zhi, Ying,De Houwer, Stephanie,Christ, Frauke,Debyser, Zeger,Neamati, Nouri
, p. 5601 - 5612 (2013/07/26)
HIV-1 integrase (IN) catalyzes the integration of viral DNA into the host genome, involving several interactions with the viral and cellular proteins. We have previously identified peptide IN inhibitors derived from the α-helical regions along the dimeric interface of HIV-1 IN. Herein, we show that appropriate hydrocarbon stapling of these peptides to stabilize their helical structure remarkably improves the cell permeability, thus allowing inhibition of the HIV-1 replication in cell culture. Furthermore, the stabilized peptides inhibit the interaction of IN with the cellular cofactor LEDGF/p75. Cellular uptake of the stapled peptide was confirmed in four different cell lines using a fluorescein-labeled analogue. Given their enhanced potency and cell permeability, these stapled peptides can serve as not only lead IN inhibitors but also prototypical biochemical probes or nanoneedles for the elucidation of HIV-1 IN dimerization and host cofactor interactions within their native cellular environment.
