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2280-68-4

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2280-68-4 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 2280-68-4 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 2,2,8 and 0 respectively; the second part has 2 digits, 6 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 2280-68:
(6*2)+(5*2)+(4*8)+(3*0)+(2*6)+(1*8)=74
74 % 10 = 4
So 2280-68-4 is a valid CAS Registry Number.

2280-68-4SDS

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 tert-butyl N-[1-[(1-amino-4-methylsulfanyl-1-oxobutan-2-yl)amino]-4-methyl-1-oxopentan-2-yl]carbamate

1.2 Other means of identification

Product number -
Other names BOC-Leu-Met-NH2

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:2280-68-4 SDS

2280-68-4Relevant articles and documents

Active Site Mapping of Human CathepsinF with Dipeptide Nitrile Inhibitors

Schmitz, Janina,Furtmann, Norbert,Ponert, Moritz,Frizler, Maxim,L?ser, Reik,Bartz, Ulrike,Bajorath, Jürgen,Gütschow, Michael

, p. 1365 - 1377 (2015/08/03)

Cleavage of the invariant chain is the key event in the trafficking pathway of major histocompatibility complex classII. CathepsinS is the major processing enzyme of the invariant chain, but cathepsinF acts in macrophages as its functional synergist which is as potent as cathepsinS in invariant chain cleavage. Dedicated low-molecular-weight inhibitors for cathepsinF have not yet been developed. An active site mapping with 52 dipeptide nitriles, reacting as covalent-reversible inhibitors, was performed to draw structure-activity relationships for the non-primed binding region of human cathepsinF. In a stepwise process, new compounds with optimized fragment combinations were designed and synthesized. These dipeptide nitriles were evaluated on human cysteine cathepsinsF, B, L, K and S. Compounds 10 (N-(4-phenylbenzoyl)-leucylglycine nitrile) and 12 (N-(4-phenylbenzoyl)leucylmethionine nitrile) were found to be potent inhibitors of human cathepsinF, with Ki values 10nM. With all dipeptide nitriles from our study, a 3D activity landscape was generated to visualize structure-activity relationships for this series of cathepsinF inhibitors. Mapping with nitriles: For human cathepsinF, low-molecular-weight inhibitors have not been developed so far. Therefore, a library of 52 dipeptide nitriles, known to interact in a covalent but reversible manner with the active site cysteine, was evaluated for cathepsinF inhibition. With the kinetic data in hand, optimized candidates were designed, synthesized, and tested to improve the activity profile as cathepsinF inhibitors.

Bombesin receptor antagonists. 5 new irreversible alkylating analogues

De Castiglione,Gozzini,Galantino,Corradi,Ciomei,Roletto,Bertolero

, p. 855 - 867 (2007/10/02)

New alkylating bombesin analogues were synthesized in order to increase their solubility and stability in aqueous solutions. The best compromise between these parameters and the biological properties (receptor binding and antagonistic activity) was achieved with 4-[bis(2-chloro-ethylamino)]benzoyl derivatives of the BN (7-14) octapeptide carrying a (13-14) reduced peptide bond independently of the presence of a His12 residue, either free or protected.

Kinetically Controlled Peptide Bond Formation in Anhydrous Alcohol Catalyzed by the Industrial Protease Alcalase

Chen, Shui-Tein,Chen, Shiah-Yun,Wang, Kung-Tsung

, p. 6960 - 6965 (2007/10/02)

The industrial alkaline protease alcalase has been found to be very stable (half life > 5 days in ethanol or 2-methyl-2-propanol) and active in alcoholic solvents (except methanol).Procedures have been developed for alcalase-catalyzed, kinetically controlled peptide bond formation in anhydrous alcohol (ethanol, 2-methyl-2-propanol).Studies of the selectivity of an alcalase-catalyzed reaction show that only L-amino acid acyl donors are substrates at the p-1 subsite of alcalase; at the p-1' subsite both D- and L-amino acid nucleophiles are substrates.Other amino compounds such as benzylamine and phenylhydrazine are good nucleophiles.Studies of the effect of the water content of the reaction solution on the yield in the synthesis of Moz-Phe-Leu-NH2 showed that the 95percent yield obtained in anhydrous 2-methyl-2-propanol was decreased to 48percent in 2-methyl-2-propanol containing 4.86percent water.

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