Lone-pair directionality in hydrogen-bond potential functions for molecular mechanics calculations: the inhibition of human carbonic anhydrase II by sulfonamides

1985 ◽  
Vol 107 (25) ◽  
pp. 7653-7658 ◽  
Author(s):  
Angelo Vedani ◽  
Jack D. Dunitz
Keyword(s):  
Hydrogen Bond ◽  
Carbonic Anhydrase ◽  
Molecular Mechanics ◽  
Lone Pair ◽  
Potential Functions ◽  
Carbonic Anhydrase Ii ◽  
Molecular Mechanics Calculations ◽  
Human Carbonic Anhydrase

scholarly journals A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

Biochemistry ◽  
2010 ◽  
Vol 49 (2) ◽  
pp. 249-251 ◽  
Author(s):  
Balendu Sankara Avvaru ◽  
Chae Un Kim ◽  
Katherine H. Sippel ◽  
Sol M. Gruner ◽  
Mavis Agbandje-McKenna ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Carbonic Anhydrase ◽  
Active Site ◽  
Carbonic Anhydrase Ii ◽  
Strong Hydrogen Bond ◽  
Human Carbonic Anhydrase

NMR Studies of Active-Site Properties of Human Carbonic Anhydrase II by Using15N-Labeled 4-Methylimidazole as a Local Probe and Histidine Hydrogen-Bond Correlations

2014 ◽  
Vol 21 (7) ◽  
pp. 2915-2929 ◽  
Author(s):  
Ilya G. Shenderovich ◽  
Stepan B. Lesnichin ◽  
Chingkuang Tu ◽  
David N. Silverman ◽  
Peter M. Tolstoy ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Carbonic Anhydrase ◽  
Active Site ◽  
Carbonic Anhydrase Ii ◽  
Nmr Studies ◽  
Human Carbonic Anhydrase

scholarly journals The Influence of Varying Fluorination Patterns on the Thermodynamics and Kinetics of Benzenesulfonamide Binding to Human Carbonic Anhydrase II

Biomolecules ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 509 ◽  
Author(s):  
Steffen Glöckner ◽  
Khang Ngo ◽  
Björn Wagner ◽  
Andreas Heine ◽  
Gerhard Klebe
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Ii ◽  
The Novel ◽  
Binding Modes ◽  
X Ray ◽  
Structure Activity ◽  
Small Set ◽  
Novel Method ◽  
Human Carbonic Anhydrase ◽  
Kinetics Of

The fluorination of lead-like compounds is a common tool in medicinal chemistry to alter molecular properties in various ways and with different goals. We herein present a detailed study of the binding of fluorinated benzenesulfonamides to human Carbonic Anhydrase II by complementing macromolecular X-ray crystallographic observations with thermodynamic and kinetic data collected with the novel method of kinITC. Our findings comprise so far unknown alternative binding modes in the crystalline state for some of the investigated compounds as well as complex thermodynamic and kinetic structure-activity relationships. They suggest that fluorination of the benzenesulfonamide core is especially advantageous in one position with respect to the kinetic signatures of binding and that a higher degree of fluorination does not necessarily provide for a higher affinity or more favorable kinetic binding profiles. Lastly, we propose a relationship between the kinetics of binding and ligand acidity based on a small set of compounds with similar substitution patterns.

Salt mediated unusual switching in the aggregation kinetic profile of human carbonic anhydrase

RSC Advances ◽  
2015 ◽  
Vol 5 (116) ◽  
pp. 95717-95726 ◽  
Author(s):  
Preeti Gupta ◽  
Shashank Deep
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Ii ◽  
Aggregation Kinetic ◽  
Kinetic Profile ◽  
Human Carbonic Anhydrase

Aggregation pathway of human carbonic anhydrase II in the presence of salt.

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