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848777-29-7

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848777-29-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 848777-29-7 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 8,4,8,7,7 and 7 respectively; the second part has 2 digits, 2 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 848777-29:
(8*8)+(7*4)+(6*8)+(5*7)+(4*7)+(3*7)+(2*2)+(1*9)=237
237 % 10 = 7
So 848777-29-7 is a valid CAS Registry Number.

848777-29-7SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name methyl (2S)-2-cyclohexyl-2-(pyrazine-2-carbonylamino)acetate

1.2 Other means of identification

Product number -
Other names (S)-methyl 2-cyclohexyl-2-(pyrazine-2-carboxamido)acetate

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:848777-29-7 SDS

848777-29-7Relevant articles and documents

Development of peptidomimetic hydroxamates as PfA-M1 and PfA-M17 dual inhibitors: Biological evaluation and structural characterization by cocrystallization

Addlagatta, Anthony,Ding, Yongzheng,Ma, Chunhua,Marapaka, Anil Kumar,Pillalamarri, Vijaykumar,Reddi, Bharati,Sankoju, Priyanka,Sijwali, Puran Singh,Sudhakar, Renu,Zhang, Guozhen,Zhang, Yingjie

supporting information, (2021/12/01)

Plasmodium parasites causing malaria have developed resistance to most of the antimalarials in use, including the artemisinin-based combinations, which are the last line of defense against malaria. This necessitates the discovery of new targets and the development of novel antimalarials. Plasmodium falciparum alanyl aminopeptidase (PfA-M1) and leucyl aminopeptidase (PfA-M17) belong to the M1 and M17 family of metalloproteases respectively and play critical roles in the asexual erythrocytic stage of development. These enzymes have been suggested as potential antimalarial drug targets. Herein we describe the development of peptidomimetic hydroxamates as PfA-M1 and PfA-M17 dual inhibitors. Most of the compounds described in this study display inhibition at sub-micromolar range against the recombinant PfA-M1 and PfA-M17. More importantly, compound 26 not only exhibits potent malarial aminopeptidases inhibitory activities (PfA-M1 Ki = 0.11 ± 0.0002 μmol/L, PfA-M17 Ki = 0.05 ± 0.005 μmol/L), but also possesses remarkable selectivity over the mammalian counterpart (pAPN Ki = 17.24 ± 0.08 μmol/L), which endows 26 with strong inhibition of the malarial parasite growth and negligible cytotoxicity on human cell lines. Crystal structures of PfA-M1 at atomic resolution in complex with four different compounds including compound 26 establish the structural basis for their inhibitory activities. Notably, the terminal ureidobenzyl group of 26 explores the S2′ region where differences between the malarial and mammalian enzymes are apparent, which rationalizes the selectivity of 26. Together, our data provide important insights for the rational and structure-based design of selective and dual inhibitors of malarial aminopeptidases that will likely lead to novel chemotherapeutics for the treatment of malaria.

Chemical and biological evaluation of dipeptidyl boronic acid proteasome inhibitors for use in prodrugs and pro-soft drugs targeting solid tumors

Milo, Lawrence J.,Lai, Jack H.,Wu, Wengen,Liu, Yuxin,Maw, Hlaing,Li, Youhua,Jin, Zhiping,Shu, Ying,Poplawski, Sarah E.,Wu, Yong,Sanford, David G.,Sudmeier, James L.,Bachovchin, William W.

experimental part, p. 4365 - 4377 (2011/09/15)

Bortezomib, a dipeptidyl boronic acid and potent inhibitor of the 26S proteasome, is remarkably effective against multiple myeloma (MM) but not against solid tumors. Dose-limiting adverse effects from "on target" inhibition of the proteasome in normal cells and tissues appear to be a key obstacle. Achieving efficacy against solid tumors therefore is likely to require making the inhibitor more selective for tumor tissue over normal tissues. The simplest strategy that might provide such tissue specificity would be to employ a tumor specific protease to release an inhibitor from a larger, noninhibitory structure. However, such release would necessarily generate an inhibitor with a free N-terminal amino group, raising a key question: Can short peptide boronic acids with N-terminal amino groups have the requisite properties to serve as warheads in prodrugs? Here we show that dipeptides of boroLeu, the smallest plausible candidates for the task, can indeed be sufficiently potent, cell-penetrating, cytotoxic, and stable to degradation by cellular peptidases to serve in this capacity.

HCV PROTEASE INHIBITORS AND USES THEREOF

-

Page/Page column 20, (2010/03/02)

This invention relates to: (a) compounds of formula I and salts thereof that, inter alia, are useful as hepatitis C virus (HCV) inhibitors; (b) intermediates useful for the preparation of such compounds and salts; (c) pharmaceutical compositions comprising such compounds and salts; and (d) methods of use of such compounds, salts, and compositions.

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