In Vitro Inhibition Studies with Homogeneous Monoamine Oxidases

1965 ◽  
Vol 8 (6) ◽  
pp. 859-862 ◽  
Author(s):  
Alfred Burger ◽  
Sakari Nara
Keyword(s):  
Monoamine Oxidases ◽  
In Vitro Inhibition ◽  
Inhibition Studies

SAR directed design and synthesis of novel β(1-4)-Glucosyltransferase inhibitors and Their In vitro inhibition studies

2002 ◽  
Vol 10 (4) ◽  
pp. 1129-1136 ◽  
Author(s):  
Asish K Bhattacharya ◽  
Florian Stolz ◽  
Jürgen Kurzeck ◽  
Wolfgang Rüger ◽  
Richard R Schmidt
Keyword(s):  
Design And Synthesis ◽  
In Vitro Inhibition ◽  
Directed Design ◽  
Inhibition Studies

Characterization and in Vitro Inhibition Studies of Bacillus anthracis FtsZ: A Potential Antibacterial Target

2014 ◽  
Vol 172 (6) ◽  
pp. 3263-3270 ◽  
Author(s):  
Hae-Chul Park ◽  
Vinayakumar Gedi ◽  
June-Haeng Cho ◽  
Jae-Wook Hyun ◽  
Kwang-Jick Lee ◽  
...  
Keyword(s):  
Bacillus Anthracis ◽  
In Vitro Inhibition ◽  
Antibacterial Target ◽  
Inhibition Studies

scholarly journals Application of Static Modeling ­­in the Prediction of In Vivo Drug–Drug Interactions between Rivaroxaban and Antiarrhythmic Agents Based on In Vitro Inhibition Studies

2017 ◽  
Vol 45 (3) ◽  
pp. 260-268 ◽  
Author(s):  
Eleanor Jing Yi Cheong ◽  
Janice Jia Ni Goh ◽  
Yanjun Hong ◽  
Gopalakrishnan Venkatesan ◽  
Yuanjie Liu ◽  
...  
Keyword(s):  
Drug Interactions ◽  
Antiarrhythmic Agents ◽  
Static Modeling ◽  
In Vitro Inhibition ◽  
Inhibition Studies

scholarly journals Synthesis and Inhibition Activity Study of Triazinyl-Substituted Amino(alkyl)-benzenesulfonamide Conjugates with Polar and Hydrophobic Amino Acids as Inhibitors of Human Carbonic Anhydrases I, II, IV, IX, and XII

2021 ◽  
Vol 22 (20) ◽  
pp. 11283
Author(s):  
Mária Bodnár Mikulová ◽  
Dáša Kružlicová ◽  
Daniel Pecher ◽  
Andrea Petreni ◽  
Claudiu T. Supuran ◽  
...  
Keyword(s):  
Amino Acids ◽  
Side Chain ◽  
Carbonic Anhydrases ◽  
Inhibition Activity ◽  
Short Reaction Time ◽  
High Affinity ◽  
Hydrophobic Amino Acids ◽  
In Vitro Inhibition ◽  
Inhibition Studies

Primary sulfonamide derivatives with various heterocycles represent the most widespread group of potential human carbonic anhydrase (hCA) inhibitors with high affinity and selectivity towards specific isozymes from the hCA family. In this work, new 4-aminomethyl- and aminoethyl-benzenesulfonamide derivatives with 1,3,5-triazine disubstituted with a pair of identical amino acids, possessing a polar (Ser, Thr, Asn, Gln) and non-polar (Ala, Tyr, Trp) side chain, have been synthesized. The optimized synthetic, purification, and isolation procedures provided several pronounced benefits such as a short reaction time (in sodium bicarbonate aqueous medium), satisfactory yields for the majority of new products (20.6–91.8%, average 60.4%), an effective, well defined semi-preparative RP-C18 liquid chromatography (LC) isolation of desired products with a high purity (>97%), as well as preservation of green chemistry principles. These newly synthesized conjugates, plus their 4-aminobenzenesulfonamide analogues prepared previously, have been investigated in in vitro inhibition studies towards hCA I, II, IV and tumor-associated isozymes IX and XII. The experimental results revealed the strongest inhibition of hCA XII with low nanomolar inhibitory constants (Kis) for the derivatives with amino acids possessing non-polar side chains (7.5–9.6 nM). Various derivatives were also promising for some other isozymes.

ChemInform Abstract: SAR-Directed Design and Synthesis of Novel β(1-4)-Glucosyltransferase Inhibitors and Their in vitro Inhibition Studies.

ChemInform ◽  
2010 ◽  
Vol 33 (20) ◽  
pp. no-no
Author(s):  
Asish k. Bhattacharya ◽  
Florian Stolz ◽  
Juergen Kurzeck ◽  
Wolfgang Rueger ◽  
Richard R. Schmidt
Keyword(s):  
Design And Synthesis ◽  
In Vitro Inhibition ◽  
Directed Design ◽  
Inhibition Studies

scholarly journals Mycobacterium tuberculosis β-Carbonic Anhydrases: Novel Targets for Developing Antituberculosis Drugs

2019 ◽  
Vol 20 (20) ◽  
pp. 5153 ◽  
Author(s):  
Aspatwar ◽  
Kairys ◽  
Rala ◽  
Parikka ◽  
Bozdag ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Pathogenic Bacteria ◽  
Bacterial Species ◽  
In Vivo Studies ◽  
Close Relative ◽  
Carbonic Anhydrases ◽  
In Vitro Inhibition ◽  
Inhibition Studies

The genome of Mycobacterium tuberculosis (Mtb) encodes three β-carbonic anhydrases (CAs, EC 4.2.1.1) that are crucial for the life cycle of the bacterium. The Mtb β-CAs have been cloned and characterized, and the catalytic activities of the enzymes have been studied. The crystal structures of two of the enzymes have been resolved. In vitro inhibition studies have been conducted using different classes of carbonic anhydrase inhibitors (CAIs). In vivo inhibition studies of pathogenic bacteria containing β-CAs showed that β-CA inhibitors effectively inhibited the growth of pathogenic bacteria. The in vitro and in vivo studies clearly demonstrated that β-CAs of not only mycobacterial species, but also other pathogenic bacteria, can be targeted for developing novel antimycobacterial agents for treating tuberculosis and other microbial infections that are resistant to existing drugs. In this review, we present the molecular and structural data on three β-CAs of Mtb that will give us better insights into the roles of these enzymes in pathogenic bacterial species. We also present data from both in vitro inhibition studies using different classes of chemical compounds and in vivo inhibition studies focusing on M. marinum, a model organism and close relative of Mtb.

Sign in / Sign up

Export Citation Format

Share Document