147529-99-5 Usage
Description
6-N-ALLOC-L-LYSINE, also known as Alloc-L-lysine, is an amino acid derivative that plays a significant role in the chemical and pharmaceutical industries. It is characterized by the presence of an Alloc (Allyloxycarbonyl) protecting group on the nitrogen atom, which is crucial for its reactivity and stability in various chemical reactions.
Uses
Used in Chemical Synthesis:
6-N-ALLOC-L-LYSINE is used as an intermediate for the large-scale synthesis of Nε-Alloc-lysine and Nε-Alloc-Nα-Fmoc-lysine. These compounds are essential in the production of various pharmaceuticals, bioactive molecules, and other specialty chemicals.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, 6-N-ALLOC-L-LYSINE is used as a building block for the development of new drugs and therapeutic agents. Its unique structure allows for the creation of novel peptide-based compounds with potential applications in treating various diseases and medical conditions.
Used in Research and Development:
6-N-ALLOC-L-LYSINE is also utilized in research and development laboratories for the synthesis of complex organic molecules and the study of various chemical reactions. Its versatility as a protected amino acid derivative makes it a valuable tool for chemists and biologists working on the design and synthesis of new molecules with specific properties and functions.
Check Digit Verification of cas no
The CAS Registry Mumber 147529-99-5 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,4,7,5,2 and 9 respectively; the second part has 2 digits, 9 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 147529-99:
(8*1)+(7*4)+(6*7)+(5*5)+(4*2)+(3*9)+(2*9)+(1*9)=165
165 % 10 = 5
So 147529-99-5 is a valid CAS Registry Number.
InChI:InChI=1/C10H18N2O4.ClH/c1-2-7-16-10(15)12-6-4-3-5-8(11)9(13)14;/h2,8H,1,3-7,11H2,(H,12,15)(H,13,14);1H/t8-;/m0./s1
147529-99-5Relevant articles and documents
Discovery of Peptidomimetic Antibody-Drug Conjugate Linkers with Enhanced Protease Specificity
Wei, Binqing,Gunzner-Toste, Janet,Yao, Hui,Wang, Tao,Wang, Jing,Xu, Zijin,Chen, Jinhua,Wai, John,Nonomiya, Jim,Tsai, Siao Ping,Chuh, Josefa,Kozak, Katherine R.,Liu, Yichin,Yu, Shang-Fan,Lau, Jeff,Li, Guangmin,Phillips, Gail D.,Leipold, Doug,Kamath, Amrita,Su, Dian,Xu, Keyang,Eigenbrot, Charles,Steinbacher, Stefan,Ohri, Rachana,Raab, Helga,Staben, Leanna R.,Zhao, Guiling,Flygare, John A.,Pillow, Thomas H.,Verma, Vishal,Masterson, Luke A.,Howard, Philip W.,Safina, Brian
, p. 989 - 1000 (2018/01/01)
Antibody-drug conjugates (ADCs) have become an important therapeutic modality for oncology, with three approved by the FDA and over 60 others in clinical trials. Despite the progress, improvements in ADC therapeutic index are desired. Peptide-based ADC linkers that are cleaved by lysosomal proteases have shown sufficient stability in serum and effective payload-release in targeted cells. If the linker can be preferentially hydrolyzed by tumor-specific proteases, safety margin may improve. However, the use of peptide-based linkers limits our ability to modulate protease specificity. Here we report the structure-guided discovery of novel, nonpeptidic ADC linkers. We show that a cyclobutane-1,1-dicarboxamide-containing linker is hydrolyzed predominantly by cathepsin B while the valine-citrulline dipeptide linker is not. ADCs bearing the nonpeptidic linker are as efficacious and stable in vivo as those with the dipeptide linker. Our results strongly support the application of the peptidomimetic linker and present new opportunities for improving the selectivity of ADCs.