303-43-5Relevant articles and documents
Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor
Chang, Catherine C. Y.,Chang, Ta-Yuan,Chen, Lei,Chen, Si-Cong,Guan, Chengcheng,Kang, Yunlu,Luo, Tuoping,Nishi, Koji,Niu, Yange,Wu, Jing-Xiang
, (2020)
Sterol O-acyltransferase 1 (SOAT1) is an endoplasmic reticulum (ER) resident, multi-transmembrane enzyme that belongs to the membrane-bound O-acyltransferase (MBOAT) family. It catalyzes the esterification of cholesterol to generate cholesteryl esters for cholesterol storage. SOAT1 is a target to treat several human diseases. However, its structure and mechanism remain elusive since its discovery. Here, we report the structure of human SOAT1 (hSOAT1) determined by cryo-EM. hSOAT1 is a tetramer consisted of a dimer of dimer. The structure of hSOAT1 dimer at 3.5 ? resolution reveals that a small molecule inhibitor CI-976 binds inside the catalytic chamber and blocks the accessibility of the active site residues H460, N421 and W420. Our results pave the way for future mechanistic study and rational drug design targeting hSOAT1 and other mammalian MBOAT family members.
Macrolactonization Reactions Driven by a Pentafluorobenzoyl Group**
Ciofini, Ilaria,Force, Guillaume,Leb?uf, David,Mayer, Robert J.,Perfetto, Anna
supporting information, p. 19843 - 19851 (2021/08/13)
Macrolactones constitute a privileged class of natural and synthetic products with a broad range of applications in the fine chemicals and pharmaceutical industry. Despite all the progress made towards their synthesis, notably from seco-acids, a macrolactonization promoter system that is effective, selective, flexible, readily available, and, insofar as possible, compatible with manifold functional groups is still lacking. Herein, we describe a strategy that relies on the formation of a mixed anhydride incorporating a pentafluorophenyl group which, due to its high electronic activation enables a convenient access to macrolactones, macrodiolides and esters with a broad versatility. Kinetic studies and DFT computations were performed to rationalize the reactivity of the pentafluorophenyl group in macrolactonization reactions.
Direct esterification of carboxylic acids with alcohols catalyzed by Iron(III) acetylacetonate complex
Weng, Shiue-Shien,Chen, Fong-Kuang,Ke, Chih-Shueh
, p. 2615 - 2621 (2013/07/26)
Direct condensation of carboxylic acids and alcohols with electronic, steric, and functional group variations was carried out using the environmentally benign, moisture-stable, inexpensive, and recoverable iron(III) acetylacetonate [Fe(acac)3] as catalyst (5 mol%). This iron salt efficiently catalyzed the esterification of several primary and secondary alcohols in refluxing xylene, without the need for a dehydration reagent. The chemoselectivity of the proposed protocol was demonstrated by the selective esterification of primary alcohol functionality in racemic 1-phenylethane-1,2- diol with benzoic acid. The esterification was also applicable to unmasked α-hydroxyacid, guasiaromatic, heterocyclic, and N-protected amino acids. Supplemental materials are available for this article. Go to the publisher's online edition of Synthetic Communications to view the free supplemental file.
