180675-08-5 Usage
Description
FMOC-ASP(OMPE)-OH is a chemical compound that serves as an organic and pharmaceutical intermediate. It is characterized by the presence of a side chain protecting group Mpe, which is bulkier than the standard tert-Butyl (tBu) group. This feature significantly helps in suppressing the side reaction of aspartimide formation, thereby improving the purity of the crude peptide and facilitating the timeand cost-intensive purification process.
Uses
Used in Organic Synthesis:
FMOC-ASP(OMPE)-OH is used as an organic synthesis intermediate for the development of various chemical compounds. Its unique structure and properties make it a valuable component in the synthesis of complex organic molecules.
Used in Pharmaceutical Research and Development:
In the pharmaceutical industry, FMOC-ASP(OMPE)-OH is utilized as a pharmaceutical intermediate. It plays a crucial role in the research and development process, contributing to the creation of new drugs and therapeutic agents.
Used in Chemical Production:
FMOC-ASP(OMPE)-OH is also employed in the chemical production process, where it serves as a key intermediate for the manufacturing of various chemicals and materials. Its bulkier side chain protecting group Mpe enhances the efficiency and purity of the production process, leading to improved final products.
Check Digit Verification of cas no
The CAS Registry Mumber 180675-08-5 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,8,0,6,7 and 5 respectively; the second part has 2 digits, 0 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 180675-08:
(8*1)+(7*8)+(6*0)+(5*6)+(4*7)+(3*5)+(2*0)+(1*8)=145
145 % 10 = 5
So 180675-08-5 is a valid CAS Registry Number.
180675-08-5Relevant articles and documents
Total Chemical Synthesis and Folding of All- l and All- d Variants of Oncogenic KRas(G12V)
Levinson, Adam M.,McGee, John H.,Roberts, Andrew G.,Creech, Gardner S.,Wang, Ting,Peterson, Michael T.,Hendrickson, Ronald C.,Verdine, Gregory L.,Danishefsky, Samuel J.
, p. 7632 - 7639 (2017/06/13)
The Ras proteins are essential GTPases involved in the regulation of cell proliferation and survival. Mutated oncogenic forms of Ras alter effector binding and innate GTPase activity, leading to deregulation of downstream signal transduction. Mutated forms of Ras are involved in approximately 30% of human cancers. Despite decades of effort to develop direct Ras inhibitors, Ras has long been considered "undruggable" due to its high affinity for GTP and its lack of hydrophobic binding pockets. Herein, we report a total chemical synthesis of all-l- and all-d-amino acid biotinylated variants of oncogenic mutant KRas(G12V). The protein is synthesized using Fmoc-based solid-phase peptide synthesis and assembled using combined native chemical ligation and isonitrile-mediated activation strategies. We demonstrate that both KRas(G12V) enantiomers can successfully fold and bind nucleotide substrates and binding partners with observable enantiodiscrimination. By demonstrating the functional competency of a mirror-image form of KRas bound to its corresponding enantiomeric nucleotide triphosphate, this study sets the stage for further biochemical studies with this material. In particular, this protein will enable mirror-image yeast surface display experiments to identify all-d peptide ligands for oncogenic KRas, providing a useful tool in the search for new therapeutics against this challenging disease target.
