110475-43-9Relevant articles and documents
An Unusual Natural Product Primary Sulfonamide: Synthesis, Carbonic Anhydrase Inhibition, and Protein X-ray Structures of Psammaplin C
Mujumdar, Prashant,Teruya, Kanae,Tonissen, Kathryn F.,Vullo, Daniela,Supuran, Claudiu T.,Peat, Thomas S.,Poulsen, Sally-Ann
, p. 5462 - 5470 (2016)
Psammaplin C is one of only two described natural product primary sulfonamides. Here we report the synthesis of psammaplin C and evaluate the inhibition profile against therapeutically relevant carbonic anhydrase (CA) zinc metalloenzymes. The compound exhibited unprecedented inhibition of an important cancer-associated isozyme, hCA XII, with a Ki of 0.79 nM. The compound also displayed good isoform selectivity for hCA XII over other CAs. We present the first reported protein X-ray crystal structures of psammaplin C in complex with human CAs. We engineered the easily crystallized hCA II enzyme to mimic both the hCA IX and hCA XII binding sites and then utilized protein X-ray crystallography to determine the binding pose of psammaplin C within the hCA II, hCA IX, and hCA XII mimic active sites, all to high resolution. This is the first time a natural product primary sulfonamide inhibitor has been assessed for inhibition and binding to CAs.
Synthesis of 2-Aminoethanesulfonamides of Betulinic and Betulonic Acids
Dubovitskii, S. N.,Komissarova, N. G.,Orlov, A. V.,Shitikova, O. V.
, (2021)
New potentially biologically active sulfonamide derivatives of pentacyclic lupane-type triterpenoids, the sulfonamide group of which was bonded to C-17 of the triterpene skeleton through an amidoethane spacer, were synthesized via conjugation of 2-aminoet
