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(3-Amino-2-hydroxy-propyl)-carbamic acid tert-butyl ester, also known as Boc-lysine, is a chemical compound derived from lysine, an essential amino acid. It is widely used in peptide synthesis and drug development as a building block for creating various peptides and proteins. Boc-lysine serves as a protecting group in organic chemistry, shielding the amino group of lysine during chemical reactions and allowing for specific modifications to be made to the molecule. As a tert-butyl ester, (3-Amino-2-hydroxy-propyl)-carbamic acid tert-butyl ester provides stability and protection to the reactive functional groups in peptides, enabling precise control over their synthesis and structure. Boc-lysine also has potential applications in pharmaceuticals, particularly in the development of new drug candidates and therapeutic agents. Overall, (3-Amino-2-hydroxy-propyl)-carbamic acid tert-butyl ester plays a critical role in the field of chemical and pharmaceutical research, contributing to advancements in the synthesis and modification of bioactive molecules.

853944-08-8

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853944-08-8 Usage

Uses

Used in Pharmaceutical Industry:
Boc-lysine is used as a building block for the synthesis of various peptides and proteins, which are essential components of many pharmaceutical products. Its role in creating specific peptide structures allows for the development of new drug candidates and therapeutic agents.
Used in Chemical Research:
Boc-lysine is used as a protecting group in organic chemistry, enabling the shielding of the amino group of lysine during chemical reactions. This allows for specific modifications to be made to the molecule, contributing to advancements in the synthesis and modification of bioactive molecules.
Used in Peptide Synthesis:
Boc-lysine is used as a key component in the synthesis of peptides, providing stability and protection to the reactive functional groups in peptides. This enables precise control over their synthesis and structure, which is crucial for the development of effective pharmaceutical products.

Check Digit Verification of cas no

The CAS Registry Mumber 853944-08-8 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 8,5,3,9,4 and 4 respectively; the second part has 2 digits, 0 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 853944-08:
(8*8)+(7*5)+(6*3)+(5*9)+(4*4)+(3*4)+(2*0)+(1*8)=198
198 % 10 = 8
So 853944-08-8 is a valid CAS Registry Number.

853944-08-8Downstream Products

853944-08-8Relevant academic research and scientific papers

METALLO-BETA-LACTAMASE INHIBITORS AND METHODS OF USE THEREOF

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Page/Page column 42-43; 59, (2019/02/06)

The present invention relates to metallo-β-lactamase inhibitor compounds of Formula (I) and pharmaceutically acceptable salts thereof, wherein Z, RA, X1, X2 and R1 are as defined herein. The present invention also relates to compositions which comprise a metallo-β-lactamase inhibitor compound of the invention or a pharmaceutically acceptable salt thereof, and a pharmaceutically acceptable carrier, optionally in combination with a beta lactam antibiotic and/or a beta-lactamase inhibitor. The invention further relates to methods for treating a bacterial infection comprising administering to a patient a therapeutically effective amount of a compound of the invention, in combination with a therapeutically effective amount of one or more β-lactam antibiotics and optionally in combination with one or more beta-lactamase inhibitor compounds. The compounds of the invention are useful in the methods described herein for overcoming antibiotic resistance.

Esterolytic peptide dendrimers with a hydrophobic core and catalytic residues at the surface

Clouet, Anthony,Darbre, Tamis,Reymond, Jean-Louis

, p. 1195 - 1204 (2007/10/03)

(3S)-4-(9-Fluorenylmethoxycarbonylamino)-3-methyl(allyloxycarbonyl) aminoethyloxyacetic acid (1) was prepared from (R)-3-aminopropane-1,2-diol and used as branching unit for the synthesis of second generation peptide dendrimers with six individually addressable variable amino acid positions. Three pairs of diastereomeric dendrimers were prepared bearing a common hydrophobic core and permutations of the catalytic triad amino acids aspartate, histidine and serine at the surface. Dendrimers with two surface histidine residues catalyzed the hydrolysis of fluorogenic 8-acyloxypyrene-1,3,6-trisulfonates in aqueous buffer pH 6.0 with rate enhancement kcat/kuncat in the 10 3 range and Michaelis-Menten constants KM in the 10 -4 M range. Substrate recognition involves electrostatic interactions, as shown by competitive inhibition of catalysis observed with pyrene-1,3,6,8-tetrasulfonate. The 4-fold to 7-fold lowering in KM between the butyryl and nonanoyl esters in the most active dendrimers provides evidence for a hydrophobic component in substrate binding, which is absent in a closely related, less active diastereomeric peptide dendrimer.

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