Carbonic anhydrase as drug target – thermodynamics and structure of inhibitor binding

2021 ◽  
pp. 1-2
Author(s):  
Franz-Josef Meyer-Almes
Keyword(s):  
Carbonic Anhydrase ◽  
Drug Target ◽  
Inhibitor Binding

Are Carbonic Anhydrases Suitable Targets to Fight Protozoan Parasitic Diseases?

2019 ◽  
Vol 25 (39) ◽  
pp. 5266-5278 ◽  
Author(s):  
Katia D'Ambrosio ◽  
Claudiu T. Supuran ◽  
Giuseppina De Simone
Keyword(s):  
Drug Resistance ◽  
Animal Models ◽  
Carbonic Anhydrase ◽  
Drug Target ◽  
Treatment Options ◽  
Parasitic Diseases ◽  
Carbonic Anhydrases ◽  
Extensive Drug Resistance ◽  
Protozoan Infections

Protozoans belonging to Plasmodium, Leishmania and Trypanosoma genera provoke widespread parasitic diseases with few treatment options and many of the clinically used drugs experiencing an extensive drug resistance phenomenon. In the last several years, the metalloenzyme Carbonic Anhydrase (CA, EC 4.2.1.1) was cloned and characterized in the genome of these protozoa, with the aim to search for a new drug target for fighting malaria, leishmaniasis and Chagas disease. P. falciparum encodes for a CA (PfCA) belonging to a novel genetic family, the η-CA class, L. donovani chagasi for a β-CA (LdcCA), whereas T. cruzi genome contains an α-CA (TcCA). These three enzymes were characterized in detail and a number of in vitro potent and selective inhibitors belonging to the sulfonamide, thiol, dithiocarbamate and hydroxamate classes were discovered. Some of these inhibitors were also effective in cell cultures and animal models of protozoan infections, making them of considerable interest for the development of new antiprotozoan drugs with a novel mechanism of action.

Inhibitor Binding Sites in the Protein Tyrosine Phosphatase SHP-2

2020 ◽  
Vol 20 (11) ◽  
pp. 1017-1030
Author(s):  
Haonan Zhang ◽  
Zhengquan Gao ◽  
Chunxiao Meng ◽  
Xiangqian Li ◽  
Dayong Shi
Keyword(s):  
Small Molecule ◽  
Protein Tyrosine Phosphatase ◽  
Binding Sites ◽  
Drug Target ◽  
Tyrosine Phosphatase ◽  
Cancer Drug ◽  
Cellular Activity ◽  
Binding Modes ◽  
Inhibitor Binding ◽  
Protein Tyrosine

Protein tyrosine phosphatase 2 (SHP-2) has long been proposed as a cancer drug target. Several small-molecule compounds with different mechanisms of SHP-2 inhibition have been reported, but none are commercially available. Pool selectivity over protein tyrosine phosphatase 1 (SHP-1) and a lack of cellular activity have hindered the development of selective SHP-2 inhibitors. In this review, we describe the binding modes of existing inhibitors and SHP-2 binding sites, summarize the characteristics of the sites involved in selectivity, and identify the suitable groups for interaction with the binding sites.

Beta-Carbonic Anhydrase 1 from Trichomonas Vaginalis as New Antiprotozoan Drug Target

2021 ◽  
Author(s):  
Claudiu T. Supuran ◽  
Anna Di Fiore ◽  
Seppo Parkkila ◽  
Giuseppina De Simone
Keyword(s):  
Carbonic Anhydrase ◽  
Drug Target ◽  
Trichomonas Vaginalis ◽  
Beta Carbonic Anhydrase ◽  
Carbonic Anhydrase 1

Characterization of human carbonic anhydrase XII stability and inhibitor binding

2013 ◽  
Vol 21 (6) ◽  
pp. 1431-1436 ◽  
Author(s):  
Vaida Jogaitė ◽  
Asta Zubrienė ◽  
Vilma Michailovienė ◽  
Joana Gylytė ◽  
Vaida Morkūnaitė ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Inhibitor Binding ◽  
Human Carbonic Anhydrase

scholarly journals Structural analysis of inhibitor binding to human carbonic anhydrase II

1998 ◽  
Vol 7 (12) ◽  
pp. 2483-2489 ◽  
Author(s):  
P. Ann Boriack-Sjodin ◽  
Samantha Zeitlin ◽  
David W. Christianson ◽  
Huang-Hsing Chen ◽  
Lori Crenshaw ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Ii ◽  
Inhibitor Binding ◽  
Human Carbonic Anhydrase
Sign in / Sign up

Export Citation Format

Share Document