19792-91-7Relevant academic research and scientific papers
Inhibition of carbonic anhydrase-II by sulfamate and sulfamide groups: An investigation involving direct thermodynamic binding measurements
Klinger, Alexandra L.,McComsey, David F.,Smith-Swintosky, Virginia,Shank, Richard P.,Maryanoff, Bruce E.
, p. 3496 - 3500 (2006)
This paper examines the relative effectiveness of bioisosteric sulfamate and sulfamide derivatives for inhibition of human carbonic anhydrase-II (CA-II) by using a direct binding assay based on the ThermoFluor method (Matulis et al. Biochemistry 2005, 44, 5258). Compounds 1-10, which represent five cognate sulfamate/ sulfamide pairs, were studied by ThermoFluor to obtain binding affinities (Ka values). The corresponding dissociation constants, Kd, provide an independent measure of CA-II activity relative to commonly used Ki values from enzyme kinetics studies. There was a sizable difference in potency between the sulfamates and sulfamides, with the sulfamides being much less potent, by factors ranging from 25 (7/8) to 1200 (3/4), These results are consistent with our recent report that sulfamides tend to be much weaker inhibitors of CA-II than their corresponding sulfamates (Maryanoff et al. J. Med. Chem. 2005, 48, 1941). Additionally, for arylsulfamides 10-12 the Kd values determined by ThermoFluor and the Ki values determined from enzyme kinetics are consistent. It appears that the sulfamide group is less suitable than the sulfamate group for obtaining potent inhibition of CA-II.
Efficient synthesis of N-oxysulfonyl formamidines through thionyl chloride-promoted reaction of sulfamates with formamides
Wusiman, Abudureheman,Hudabaierdi, Ruzeahong
supporting information, p. 2015 - 2021 (2017/10/13)
N-Oxysulfonyl formamidine derivatives have been efficiently synthesized under mild conditions through direct condensation of various sulfamates and formamides in the presence of thionyl chloride. The scope of this reaction was investigated, and a plausible mechanism was proposed. The resulting N-oxysulfonyl formamidines can be converted to sulfamates through appropriate deprotection.
N-Sulfonylcarboxamide as an Oxidizing Directing Group for Ruthenium-Catalyzed C–H Activation/Annulation
Petrova, Elina,Rasina, Dace,Jirgensons, Aigars
supporting information, p. 1773 - 1779 (2017/04/13)
N-Sulfonylcarboxamides can act as both a directing group for C–H activation and an internal oxidant in the Ru-catalyzed annulation reaction with alkynes to give isoquinolones. Of all of the N-sulfonylcarboxamides that were studied, the N-(2,6-difluorophenyl)sulfonamide derivatives were found to be the most efficient and led to the formation of an unstable sulfinate byproduct that decomposed into 1,3-difluorobenzene under the reaction conditions. The described isoquinolone synthesis provides an alternative to the currently known traceless annulations of hydroxamic acid and sulfoximine derivatives.
Selective intermolecular amination of C-H bonds at tertiary carbon centers
Roizen, Jennifer L.,Zalatan, David N.,Du Bois
supporting information, p. 11343 - 11346 (2013/11/06)
C-H insertion: A method for intermolecular amination of tertiary C-H bonds is described that uses limiting amounts of substrate and a convenient phenol-derived nitrogen source. Structure-selectivity and mechanistic studies suggest that steric interaction between the substrate and active oxidant is the principal determinant of product selectivity. Copyright
N-(tert -butoxycarbonyl)- N -[(triethylenediammonium)sulfonyl]azanide: A convenient sulfamoylation reagent for alcohols
Armitage, Ian,Berne, Alexander M.,Elliott, Eric L.,Fu, Mingkun,Hicks, Frederick,McCubbin, Quentin,Zhu, Lei
supporting information; experimental part, p. 2626 - 2629 (2012/07/28)
A convenient and efficient procedure is described for the sulfamoylation of alcohols using N-(tert-butoxycarbonyl)-N-[(triethylenediammonium)sulfonyl] azanide (1). The ambient temperature stable reagent 1 reacts with phenols as well as primary and secondary alcohols to give high to modest yields. The relative reaction rate of substrates was determined (primary > phenol > secondary ? tertiary). The reagent's utility as a selective sulfamoylation reagent with polyols is also demonstrated.
Intermolecular amination of allyl alcohols with sulfamates: Effective utilization of mercuric catalyst
Yamamoto, Hirofumi,Ho, Elisabeth,Sasaki, Ikuo,Mitsutake, Mizuho,Takagi, Yuichi,Imagawa, Hiroshi,Nishizawa, Mugio
supporting information; experimental part, p. 2417 - 2420 (2011/06/10)
Herein, we describe the intermolecular amination of allyl alcohols with sulfamates, which have been underutilized as nitrogen nucleophiles for allylic amination. Methyl sulfamate is a good nucleophile in the presence of mercuric triflate and efficiently generates monoallylation products in excellent yield at room temperature. Furthermore, the solid-supported mercuric catalyst silaphenyl mercuric triflate also showed remarkable catalytic activity for the allylic amination. Intermolecular amination of allyl alcohol with sulfamate as a modifiable nitrogen nucleophile is presented. Mercuric reagents act as highly efficient catalyst for the allylic amination, and the procedure was applied to the preparation of various amine derivatives. In many cases, the reaction can be carried out at room temperature and is applicable to a large range of allylic alcohols to give the monoallylated products in excellent yield. Copyright
A novel class of antihyperlipidemic agents with low density lipoprotein receptor up-regulation via the adaptor protein autosomal recessive hypercholesterolemia
Asano, Shigehiro,Ban, Hitoshi,Tsuboya, Norie,Uno, Shinsaku,Kino, Kouichi,Ioriya, Katsuhisa,Kitano, Masafumi,Ueno, Yoshihide
experimental part, p. 3284 - 3295 (2010/09/05)
We have previously reported compound 2 as a inhibitor of acyl-coenzyme A:cholesterol O-acyltransferase (ACAT) and up-regulator of the low density lipoprotein receptor (LDL-R) expression. In this study we focused on compound 2, a unique LDL-R up-regulator,
Elimination mechanisms in the aminolysis of sulfamate esters of the type NH2SO2OC6H2X - Models of enzyme inhibitors
Spillane, William J.,O'Byrne, Andrew,McCaw, Cheryl J. A.
experimental part, p. 4200 - 4205 (2009/04/11)
The kinetics of the reaction of 4-nitrophenyl sulfamate NH 2SO2OC6H4NO2-4 (1a) in acetonitrile (ACN) with a series of pyridines (pKa range ca. 8 units) and alicyclic amines (pKa range ca. 3.6 units) has been studied in the presence of excess amine at various temperatures. The compounds 1a-1f are important as model substrates for the medicinally important sulfamate esters 667-coumate and emate and analogues. Pseudo-first-order rate constants (k obsd.) have been obtained mainly by the release of 4-nitrophenol/4-nitrophenoxide. Slopes of plots of kobsd. vs. [amine] gave second-order rate constants (k2), and Broensted plots were biphasic for the aminolysis (with alicyclic amines) with an initial slope β1 = 0.53 and a subsequent slope β2 = 0.19. The change in slope occurs near the first pKa of 1a (17.9) in ACN. Leaving-group effects were probed by using the same series of phenyl sulfamates, i.e. 1a-f and the alicyclic amines N-formylpiperazine and pyrrolidine. The reactions were considered to be dissociative in nature involving E2- and E1cB- type mechanisms with the phenyl sulfamate anion 2 being involved in pyridine and in the weaker alicyclic amines (β1 segment) and a phenyl sulfamate dianion 3 being involved with the stronger alicyclic bases (β2 segment). The calculation of Leffler indices (α) for bond-forming (base...H+) and bond-breaking (S-OAr) steps allows fuller interpretation of the mechanisms occurring, which are seen as having the N-sulfonylamines, HN=SO2 and -N=SO2 on the reaction pathways leading to products. Wiley-VCH Verlag GmbH & Co. KGaA, 2008.
Ground state structures of sulfate monoesters and sulfamates reveal similar reaction coordinates for sulfuryl and sulfamyl transfer
Denehy, Emma,White, Jonathan M.,Williams, Spencer J.
, p. 314 - 316 (2008/02/08)
Structure/reactivity and structure/structure correlations of 5 sulfate monoesters and 11 sulfamate esters determined by low temperature X-ray crystallography reveal similar ground state deformations that suggest similar reaction coordinates for sulfuryl and sulfamyl group transfer. The Royal Society of Chemistry 2006.
Synthesis and evaluation of general mechanism-based inhibitors of sulfatases based on (difluoro)methyl phenyl sulfate and cyclic phenyl sulfamate motifs
Hanson, Sarah R.,Whalen, Lisa J.,Wong, Chi-Huey
, p. 8386 - 8395 (2008/02/05)
Several model mechanism-based inhibitors (MbIs) were designed and evaluated for their ability to inhibit sulfatases. The MbI motifs were based on simple aromatic sulfates, which are known to be commonly accepted substrates across this highly conserved enzyme class, so that they might be generally useful for sulfatase labeling studies. (Difluoro)methyl phenol sulfate analogs, constructed to release a reactive quinone methide trap, were not capable of irreversibly inactivating the sulfatase active site. On the other hand, the cyclic sulfamates (CySAs) demonstrated inhibition profiles consistent with an active site-directed mode of action. These molecules represent a novel scaffold for labeling sulfatases and for probing their catalytic mechanism.
