4668-38-6 Usage
Uses
Used in Pharmaceutical Industry:
Z-ASN-OET is used as a building block for the synthesis of peptides and proteins, contributing to the development of a variety of pharmaceuticals and biologically active compounds. Its role in the creation of these compounds is crucial for advancing medical treatments and therapies.
Used in Research and Development:
Z-ASN-OET is employed as a research tool for studying enzyme-substrate interactions, which is essential for understanding the mechanisms of various biological processes and the development of novel drugs. Its use in this capacity aids in the discovery of new therapeutic agents and the improvement of existing ones.
Used in Drug Solubility and Bioavailability Enhancement:
Z-ASN-OET is used to improve the solubility and bioavailability of certain drugs, which can be particularly beneficial for compounds with poor water solubility. By enhancing these properties, Z-ASN-OET can contribute to the effectiveness and safety of pharmaceutical formulations.
Check Digit Verification of cas no
The CAS Registry Mumber 4668-38-6 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 4,6,6 and 8 respectively; the second part has 2 digits, 3 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 4668-38:
(6*4)+(5*6)+(4*6)+(3*8)+(2*3)+(1*8)=116
116 % 10 = 6
So 4668-38-6 is a valid CAS Registry Number.
InChI:InChI=1/C14H18N2O5/c1-2-20-13(18)11(8-12(15)17)16-14(19)21-9-10-6-4-3-5-7-10/h3-7,11H,2,8-9H2,1H3,(H2,15,17)(H,16,19)/t11-/m0/s1
4668-38-6Relevant articles and documents
Chemo-enzymatic preparation of chiral 3-aminopyrrolidine derivatives
Iding, Hans,Wirz, Beat,Rogers-Evans, Mark
, p. 647 - 653 (2007/10/03)
A new simple method for the enantioselective enzymatic hydrolysis of N-protected D-asparagine esters suitable for the use on the preparative scale is presented. Due to major obstacles observed under conventional reaction conditions - racemization of the retained ester and a strong enzyme inactivation - a comparatively low pH together with an organic co-solvent had to be employed. Under these conditions, nearly all tested proteases demonstrated good activity and excellent enantioselectivity giving access to the corresponding D-esters and L-asparagines in high optical purities (>95% ee) and good chemical yields (>40%). From the unnatural D-asparagine derivative, sequential cyclization, selective deprotection and reduction yielded efficiently benzyl protected (R)-3-aminopyrrolidine, a homo-chiral building block utilized in numerous drug candidates.
