Simple alcohols are found widely in nature. Ethanol is the most prominent because it is the product of fermentation, a major energy-producing pathway. 141699-55-0, formula is C8H15NO3, Other simple alcohols, chiefly fusel alcohols, are formed in only trace amounts. More complex alcohols however are pervasive, as manifested in sugars, some amino acids, and fatty acids. , Electric Literature of 141699-55-0
Falgueyret, Jean-Pierre;Oballa, Renata M.;Okamoto, Osamu;Wesolowski, Gregg;Aubin, Yves;Rydzewski, Robert M.;Prasit, Peppi;Riendeau, Denis;Rodan, Sevgi B.;Percival, M. David research published 《 Novel, Nonpeptidic Cyanamides as Potent and Reversible Inhibitors of Human Cathepsins K and L》, the research content is summarized as follows. Compounds containing a 1-cyanopyrrolidinyl ring were identified as potent and reversible inhibitors of cathepsins K and L. The original lead compound I inhibits cathepsins K and L with IC50 values of 0.37 and 0.45 μM, resp. Modification of compound I by replacement of the quinoline moiety led to the synthesis of N-(1-cyano-3-pyrrolidinyl)benzenesulfonamide (2). Compound II was found to be a potent inhibitor of cathepsins K and L with a Ki value of 50 nM for cathepsin K. Replacement of the 1-cyanopyrrolidine of compound II by a 1-cyanoazetidine increased the potency of the inhibitor by 10-fold. This increase in potency is probably due to an enhanced chem. reactivity of the compound toward the thiolate of the active site of the enzyme. This is demonstrated when the assay is performed in the presence of glutathione at pH 7.0 which favors the formation of a GSH thiolate anion. Under these assay conditions, there is a loss of potency in the 1-cyanoazetidine series due to the formation of an inactive complex between the GSH thiolate and the 1-cyanoazetidine inhibitors. 1-Cyanopyrrolidinyl inhibitors exhibited time-dependent inhibition which allowed us to determine the association and dissociation rate constants with human cathepsin K. The kinetic data obtained showed that the increase of potency observed between different 1-cyanopyrrolidinyl inhibitors is due to an increase of kon values and that the association of the compound with the enzyme fits an apparent one-step mechanism. 13C NMR experiments performed with the enzyme papain showed that compound 2 forms a covalent isothiourea ester adduct with the enzyme. As predicted by the kinetic anal., the addition of the irreversible inhibitor E64 to the enzyme-cyanopyrrolidinyl complex totally abolished the signal of the isothiourea bond as observed by 13C NMR, thereby demonstrating that the formation of the covalent bond with the active site cysteine residue is reversible. Finally, compound II inhibits bone resorption in an in vitro assay involving rabbit osteoclasts and bovine bone with an IC50 value of 0.7 μM. 1-Cyanopyrrolidine represents a new class of nonpeptidic compounds that inhibit cathepsin K and L activity and proteolysis of bone collagen.
Electric Literature of 141699-55-0, Tert-butyl 3-hydroxyazetidine-1-carboxylate is a useful research compound. Its molecular formula is C8H15NO3 and its molecular weight is 173.21 g/mol. The purity is usually 95%.
Tert-butyl 3-hydroxyazetidine-1-carboxylate has been shown to be a good substrate for the preparation of N-protected amino alcohols and amines by the process of reductive amination. In this synthesis, tert-butyl azetidinium chloride is used as a catalyst in the reaction with sodium hydroxide. The tert-butyl group can be removed using ammonium hydroxide in the presence of a base such as triethylamine. This reaction can be performed on a large scale, making it useful in the manufacture of pharmaceuticals. The efficiency and solubility of this process make it suitable for use as an introduction to other processes involving N-protected amino alcohols or amines., 141699-55-0.
Referemce:
Alcohol – Wikipedia,
Alcohols – Chemistry LibreTexts