Cargando…

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

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...

Descripción completa

Detalles Bibliográficos
Autores principales:	Glöckner, Steffen, Ngo, Khang, Wagner, Björn, Heine, Andreas, Klebe, Gerhard
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2020
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7226267/ https://www.ncbi.nlm.nih.gov/pubmed/32230853 http://dx.doi.org/10.3390/biom10040509

Ejemplares similares

A Proof-of-Concept Fragment Screening of a Hit-Validated 96-Compounds Library against Human Carbonic Anhydrase II
por: Glöckner, Steffen, et al.
Publicado: (2020)

Intrinsic Thermodynamics and Structure Correlation of Benzenesulfonamides with a Pyrimidine Moiety Binding to Carbonic Anhydrases I, II, VII, XII, and XIII
por: Kišonaitė, Miglė, et al.
Publicado: (2014)

Benzylaminoethyureido-Tailed Benzenesulfonamides: Design, Synthesis, Kinetic and X-ray Investigations on Human Carbonic Anhydrases
por: Ali, Majid, et al.
Publicado: (2020)

4-Amino-substituted Benzenesulfonamides as Inhibitors of Human Carbonic Anhydrases
por: Rutkauskas, Kęstutis, et al.
Publicado: (2014)

Carbonic anhydrase inhibition with a series of novel benzenesulfonamide-triazole conjugates
por: El-Gazzar, Marwa G., et al.
Publicado: (2018)

Diversely N-substituted benzenesulfonamides dissimilarly bind to human carbonic anhydrases: crystallographic investigations of N-nitrosulfonamides
por: Angeli, Andrea, et al.
Publicado: (2023)

Two Methods, One Goal: Structural Differences between Cocrystallization and Crystal Soaking to Discover Ligand Binding Poses
por: Wienen‐Schmidt, Barbara, et al.
Publicado: (2020)

Beta and Gamma Amino Acid-Substituted Benzenesulfonamides as Inhibitors of Human Carbonic Anhydrases
por: Balandis, Benas, et al.
Publicado: (2022)

Benzenesulfonamides Incorporating Hydantoin Moieties Effectively Inhibit Eukaryoticand Human Carbonic Anhydrases
por: Abdoli, Morteza, et al.
Publicado: (2022)

Carbonic Anhydrase Inhibition Activities of Schiff’s Bases Based on Quinazoline-Linked Benzenesulfonamide
por: El-Azab, Adel S., et al.
Publicado: (2022)

Intrinsic thermodynamics of ethoxzolamide inhibitor binding to human carbonic anhydrase XIII
por: Baranauskienė, Lina, et al.
Publicado: (2012)

Ligand-Induced Protein Mobility in Complexes of Carbonic Anhydrase II and Benzenesulfonamides with Oligoglycine Chains
por: Krishnamurthy, Vijay M., et al.
Publicado: (2013)

Probing the chemical interaction space governed by 4-aminosubstituted benzenesulfonamides and carbonic anhydrase isoforms
por: Rasti, Behnam, et al.
Publicado: (2018)

Thiazide and other Cl-benzenesulfonamide-bearing clinical drug affinities for human carbonic anhydrases
por: Baranauskiene, Lina, et al.
Publicado: (2021)

4-(3-Alkyl/benzyl-guanidino)benzenesulfonamides as selective carbonic anhydrase VII inhibitors
por: Abdoli, Morteza, et al.
Publicado: (2022)

Design and synthesis of some new benzoylthioureido benzenesulfonamide derivatives and their analogues as carbonic anhydrase inhibitors
por: Oudah, Khulood H., et al.
Publicado: (2022)

Uracil as a Zn-Binding Bioisostere of the Allergic Benzenesulfonamide in the Design of Quinoline–Uracil Hybrids as Anticancer Carbonic Anhydrase Inhibitors
por: El-Kalyoubi, Samar A., et al.
Publicado: (2022)

Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding
por: Smirnov, Alexey, et al.
Publicado: (2018)

Which Properties Allow Ligands to Open and Bind to the Transient Binding Pocket of Human Aldose Reductase?
por: Sandner, Anna, et al.
Publicado: (2021)

Inhibition of bacterial α-, β- and γ-class carbonic anhydrases with selenazoles incorporating benzenesulfonamide moieties
por: Angeli, Andrea, et al.
Publicado: (2018)

Synthesis, Molecular Docking Analysis, and Carbonic Anhydrase Inhibitory Evaluations of Benzenesulfonamide Derivatives Containing Thiazolidinone
por: Zhang, Zuo-Peng, et al.
Publicado: (2019)

Hypoxia-Activated Prodrug Derivatives of Carbonic Anhydrase Inhibitors in Benzenesulfonamide Series: Synthesis and Biological Evaluation
por: Anduran, Emilie, et al.
Publicado: (2020)

Screening of benzenesulfonamide in combination with chemically diverse fragments against carbonic anhydrase by differential scanning fluorimetry
por: Krasavin, Mikhail, et al.
Publicado: (2019)

Synthesis and pharmacological effects of novel benzenesulfonamides carrying benzamide moiety as carbonic anhydrase and acetylcholinesterase inhibitors
por: TUĞRAK, Mehtap, et al.
Publicado: (2020)

Discovery of Novel Hydroxyimine-Tethered Benzenesulfonamides as Potential Human Carbonic Anhydrase IX/XII Inhibitors
por: Peerzada, Mudasir Nabi, et al.
Publicado: (2023)

Evaluation of Thio- and Seleno-Acetamides Bearing Benzenesulfonamide as Inhibitor of Carbonic Anhydrases from Different Pathogenic Bacteria
por: Angeli, Andrea, et al.
Publicado: (2020)

Fragment Binding to Kinase Hinge: If Charge Distribution and Local pK (a) Shifts Mislead Popular Bioisosterism Concepts
por: Oebbeke, Matthias, et al.
Publicado: (2020)

Appraisal of anti-protozoan activity of nitroaromatic benzenesulfonamides inhibiting carbonic anhydrases from Trypanosoma cruzi and Leishmania donovani
por: Nocentini, Alessio, et al.
Publicado: (2019)

Design, Synthesis and Biological Assessment of Rhodanine-Linked Benzenesulfonamide Derivatives as Selective and Potent Human Carbonic Anhydrase Inhibitors
por: Swain, Baijayantimala, et al.
Publicado: (2022)

Design, synthesis, and carbonic anhydrase inhibition activities of Schiff bases incorporating benzenesulfonamide scaffold: Molecular docking application
por: El-Azab, Adel S., et al.
Publicado: (2023)

Synthesis and biological evaluation of novel 3-(quinolin-4-ylamino)benzenesulfonamides as carbonic anhydrase isoforms I and II inhibitors
por: Al-Sanea, Mohammad M., et al.
Publicado: (2019)

Design, synthesis and mechanistic study of new benzenesulfonamide derivatives as anticancer and antimicrobial agents via carbonic anhydrase IX inhibition
por: Nemr, Mohamed T. M., et al.
Publicado: (2021)

Benzenesulfonamide derivatives as Vibrio cholerae carbonic anhydrases inhibitors: a computational-aided insight in the structural rigidity-activity relationships
por: Fantacuzzi, Marialuigia, et al.
Publicado: (2023)

Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
por: Schiebel, Johannes, et al.
Publicado: (2018)

Benzenesulfonamides with different rigidity-conferring linkers as carbonic anhydrase inhibitors: an insight into the antiproliferative effect on glioblastoma, pancreatic, and breast cancer cells
por: Liguori, Francesco, et al.
Publicado: (2022)

Potent carbonic anhydrase I, II, IX and XII inhibition activity of novel primary benzenesulfonamides incorporating bis-ureido moieties
por: Tekeli, Tuba, et al.
Publicado: (2023)

Intracellular Binding/Unbinding Kinetics of Approved Drugs to Carbonic Anhydrase II Observed by in-Cell NMR
por: Luchinat, Enrico, et al.
Publicado: (2020)

Novel Diamide-Based Benzenesulfonamides as Selective Carbonic Anhydrase IX Inhibitors Endowed with Antitumor Activity: Synthesis, Biological Evaluation and In Silico Insights
por: Abdelrahman, Mohamed A., et al.
Publicado: (2019)

Synthetic Strategies and Computational Inhibition Activity Study for Triazinyl-Substituted Benzenesulfonamide Conjugates with Polar and Hydrophobic Amino Acids as Inhibitors of Carbonic Anhydrases
por: Mikulová, Mária Bodnár, et al.
Publicado: (2020)

Identification of Novel and Potent Indole-Based Benzenesulfonamides as Selective Human Carbonic Anhydrase II Inhibitors: Design, Synthesis, In Vitro, and In Silico Studies
por: Elkamhawy, Ahmed, et al.
Publicado: (2022)

Cannot write session to /tmp/vufind_sessions/sess_l6uetg74lhe6gj91smetsm425j