Nonaromatic Sulfonamide Group as an Ideal Anchor for Potent Human Carbonic Anhydrase Inhibitors:  Role of Hydrogen-Bonding Networks in Ligand Binding and Drug Design

2002 ◽  
Vol 45 (17) ◽  
pp. 3583-3587 ◽  
Author(s):  
Francesco Abbate ◽  
Claudiu T. Supuran ◽  
Andrea Scozzafava ◽  
Pierluigi Orioli ◽  
Milton T. Stubbs ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Drug Design ◽  
Carbonic Anhydrase ◽  
Ligand Binding ◽  
Carbonic Anhydrase Inhibitors ◽  
Hydrogen Bonding Networks ◽  
Human Carbonic Anhydrase ◽  
Sulfonamide Group

scholarly journals Hydrophobic Substituents of the Phenylmethylsulfamide Moiety Can Be Used for the Development of New Selective Carbonic Anhydrase Inhibitors

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Giuseppina De Simone ◽  
Ginta Pizika ◽  
Simona Maria Monti ◽  
Anna Di Fiore ◽  
Jekaterina Ivanova ◽  
...  
Keyword(s):  
Drug Design ◽  
Carbonic Anhydrase ◽  
Van Der Waals ◽  
Van Der Waals Interactions ◽  
Zinc Binding ◽  
Binding Mechanism ◽  
Carbonic Anhydrase Inhibitors ◽  
X Ray ◽  
Human Carbonic Anhydrase ◽  
Hydrophobic Cleft

A new series of compounds containing a sulfamide moiety as zinc-binding group (ZBG) has been synthesized and tested for determining inhibitory properties against four human carbonic anhydrase (hCA) isoforms, namely, CAs I, II, IX, and XII. The X-ray structure of the cytosolic dominant isoform hCA II in complex with the best inhibitor of the series has also been determined providing further insights into sulfamide binding mechanism and confirming that such zinc-binding group, if opportunely derivatized, can be usefully exploited for obtaining new potent and selective CAIs. The analysis of the structure also suggests that for drug design purposes the but-2-yn-1-yloxy moiety tail emerges as a very interesting substituent of the phenylmethylsulfamide moiety due to its capability to establish strong van der Waals interactions with a hydrophobic cleft on the hCA II surface, delimited by residues Phe131, Val135, Pro202, and Leu204. Indeed, the complementarity of this tail with the cleft suggests that different substituents could be used to discriminate between isoforms having clefts with different sizes.

In-Silico Analysis of Chromone Containing Sulfonamide Derivatives as Human Carbonic Anhydrase Inhibitors

2013 ◽  
Vol 9 (4) ◽  
pp. 608-616 ◽  
Author(s):  
Zaheer Ul-Haq ◽  
Saman Usmani ◽  
Uzma Mahmood ◽  
Mariya al-Rashida ◽  
Ghulam Abbas
Keyword(s):  
Carbonic Anhydrase ◽  
In Silico ◽  
In Silico Analysis ◽  
Carbonic Anhydrase Inhibitors ◽  
Human Carbonic Anhydrase ◽  
Silico Analysis

Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant

Biochemistry ◽  
1989 ◽  
Vol 28 (19) ◽  
pp. 7913-7918 ◽  
Author(s):  
Chingkuang Tu ◽  
David N. Silverman ◽  
Cecilia Forsman ◽  
Bengt Harald Jonsson ◽  
Sven Lindskog
Keyword(s):  
Carbonic Anhydrase ◽  
Catalytic Mechanism ◽  
Carbonic Anhydrase Ii ◽  
Site Specific ◽  
Human Carbonic Anhydrase ◽  
A Site

Understanding the role of hydrogen bonding in Brønsted acidic ionic liquid-catalyzed transesterification: a combined theoretical and experimental investigation

2016 ◽  
Vol 18 (48) ◽  
pp. 32723-32734 ◽  
Author(s):  
Kaixin Li ◽  
Yibo Yan ◽  
Jun Zhao ◽  
Junxi Lei ◽  
Xinli Jia ◽  
...  
Keyword(s):  
Experimental Investigation ◽  
Ionic Liquid ◽  
Hydrogen Bonding ◽  
Catalytic Activity ◽  
Ionic Liquids ◽  
Acidic Ionic Liquid ◽  
Brønsted Acidic Ionic Liquid ◽  
Acidic Ionic Liquids ◽  
Hydrogen Bonding Networks

The intra- and inter-hydrogen bonding networks that govern the catalytic activity of Brønsted acidic ionic liquids were identified.

Out of the active site binding pocket for carbonic anhydrase inhibitors

2015 ◽  
Vol 51 (2) ◽  
pp. 302-305 ◽  
Author(s):  
Katia D'Ambrosio ◽  
Simone Carradori ◽  
Simona M. Monti ◽  
Martina Buonanno ◽  
Daniela Secci ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Active Site ◽  
Binding Pocket ◽  
Carbonic Anhydrase Ii ◽  
Carbonic Anhydrase Inhibitors ◽  
Human Carbonic Anhydrase ◽  
Site Binding

2-Benzylsulfinylbenzoic acid binds to human carbonic anhydrase II in a mode completely different from any other class of carbonic anhydrase inhibitors investigated so far.

scholarly journals Role of Hydrophilic Residues in Proton Transfer during Catalysis by Human Carbonic Anhydrase II†‡

Biochemistry ◽  
2008 ◽  
Vol 47 (46) ◽  
pp. 12028-12036 ◽  
Author(s):  
Jiayin Zheng ◽  
Balendu Sankara Avvaru ◽  
Chingkuang Tu ◽  
Robert McKenna ◽  
David N. Silverman
Keyword(s):  
Carbonic Anhydrase ◽  
Proton Transfer ◽  
Carbonic Anhydrase Ii ◽  
Human Carbonic Anhydrase ◽  
Hydrophilic Residues
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