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4892-10-8

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4892-10-8 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 4892-10-8 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 4,8,9 and 2 respectively; the second part has 2 digits, 1 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 4892-10:
(6*4)+(5*8)+(4*9)+(3*2)+(2*1)+(1*0)=108
108 % 10 = 8
So 4892-10-8 is a valid CAS Registry Number.
InChI:InChI=1/C27H28N2O5/c1-33-26(31)24(18-21-13-7-3-8-14-21)28-25(30)23(17-20-11-5-2-6-12-20)29-27(32)34-19-22-15-9-4-10-16-22/h2-16,23-24H,17-19H2,1H3,(H,28,30)(H,29,32)/t23-,24-/m0/s1

4892-10-8Relevant articles and documents

An efficient amide-forming reaction using tributyltrichloromethylphosphonium chloride

Lorca,Kurosu

, p. 469 - 473 (2001)

An efficient and expeditious amide-forming reaction is described via a combination of tributylphosphine and carbon tetrachloride (in situ generation of tributyltrichloromethylphosphonium chloride) in the absence of tertiary amines.

Mechanochemical Synthesis of Dipeptides Using Mg-Al Hydrotalcite as Activating Agent under Solvent-Free Reaction Conditions

Landeros, José M.,Juaristi, Eusebio

, p. 687 - 694 (2017/02/05)

Given the high demand for green and sustainable synthetic methods for the formation of amides and peptidic bonds, herein we report the efficient, solvent-free mechanochemical synthesis of dipeptides from N-protected amino acids and amino acid methyl ester

Synthesis, bioactivity, docking and molecular dynamics studies of furan-based peptides as 20s proteasome inhibitors

Sun, Qi,Xu, Bo,Niu, Yan,Xu, Fengrong,Liang, Lei,Wang, Chao,Yu, Jiapei,Yan, Gang,Wang, Wei,Jin, Hongwei,Xu, Ping

, p. 498 - 510 (2015/03/18)

Proteasome inhibitors are promising compounds for a number of therapies, including cardiovascular and eye diseases, diabetes, and cancers. We previously reported a series of furanbased peptidic inhibitors with moderate potencies against the proteasome b5 subunit, hypothesizing that the C-terminal furyl ketone motif could form a covalent bond with the catalytic residue, threonine 1. In this context, we describe further optimizations of the furan-based peptides, and a series of dipeptidic and tripeptidic inhibitors were designed and synthesized, aiming at improved potency and better solubility. Most of the tripeptidic inhibitors demonstrated improved potency and selectivity as b5 subunit inhibitors in both enzymatic and cellular assays, and good antineoplastic activities in various tumor cell lines were also observed. However, no inhibitory effects were observed for the dipeptidic compounds, which led us to presume that a noncovalent binding mode is adopted. Docking studies and molecular dynamics simulations were carried out to verify this presumption, with results showing that the distance between the furyl ketone motif and Thr1 is slightly too long to form covalent bond.

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