Synthesis of and Molecular Docking Studies of Azomethine- Tethered Sulfonamides as Carbonic Anhydrase II & 15-Lipoxygenase Inhibitors

2021 ◽  
pp. 130821
Author(s):  
Aamer Saeed ◽  
Syeda Abida Ejaz ◽  
Anwar Ul-Hamid ◽  
Hesham R. El-Seedi ◽  
Jamshed Iqbal
Keyword(s):  
Molecular Docking ◽  
Carbonic Anhydrase ◽  
Docking Studies ◽  
Carbonic Anhydrase Ii ◽  
Lipoxygenase Inhibitors ◽  
Molecular Docking Studies

Inhibition Profiling of Urease and Carbonic Anhydrase II by High- Throughput Screening and Molecular Docking Studies of Structurally Diverse Organic Compounds

2020 ◽  
Vol 17 ◽  
Author(s):  
Majid Ali ◽  
Syed Majid Bukhari ◽  
Asma Zaidi ◽  
Farhan A. Khan ◽  
Umer Rashid ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Carbonic Anhydrase ◽  
Metal Complexes ◽  
Organic Compounds ◽  
High Throughput ◽  
High Throughput Screening ◽  
Docking Studies ◽  
Carbonic Anhydrase Ii ◽  
Molecular Docking Studies ◽  
Ic50 Values

Background:: Structurally diverse organic compounds and available drugs were screened against urease and carbonic anhydrase II in a formulation acceptable for high-throughput screening. Objective: The study was conducted to find out potential inhibitors of urease and carbonic anhydrase II. Methods:: Quantification of the possible HITs was carried out by determining their IC50 values. Results and Discussion:: of several screened compounds including derivatives of oxadiazole, coumarins, chromane-2, 4- diones and metal complexes of cysteine-omeprazole showed promising inhibitory activities with IC50 ranging from 47 μM to 412 μM against the urease. The interactions of active compounds with active sites of enzymes were investigated through molecular docking studies which revealed that (R)-1-(4-amino-4-(5-(thiophen-2-yl)-1,3,4-oxadiazol-2-yl) butyl) guanidine possessing IC50 of 47 μM, interacts with one of the nickel metal atom of urease besides further interactions as predictable hydrogen bonds with KCX490, Asp633, His492, His407 and His409 along with Ala440 and 636. Bi-ligand metal complexes of 4-aminoantipyrine based Schiff bases showed activation of urease with AC50 ranging from 68 μM to 112 μM. Almost 21 compounds with varying functional groups including pyrimidines, oxadiazoles, imidazoles, hydrazides and tin based compounds were active carbonic anhydrase II inhibitors presenting 98 μM to 390 μM IC50 values. Several N-substituted sulfonamide derivatives were inactive against carbonic anhydrase II. Conclusion:: Among all the screened compounds, highly active inhibitor of carbonic anhydrase II was (4-(3- hydroxyphenyl)-6-phenyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl)phenyl) methanone with IC50 of 98.0 μM. This particular compound showed metallic interaction with Zn ion of carbonic anhydrase II through hydroxyl group of phenyl ring.

New thiopyrimidine-benzenesulfonamide conjugates as selective carbonic anhydrase II inhibitors: synthesis, in vitro biological evaluation, and molecular docking studies

2020 ◽  
Vol 28 (5) ◽  
pp. 115329 ◽  
Author(s):  
Heba T. Abdel-Mohsen ◽  
Ahmed M. El Kerdawy ◽  
Mohamed A. Omar ◽  
Emanuela Berrino ◽  
Ahmed S. Abdelsamie ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Carbonic Anhydrase ◽  
Docking Studies ◽  
Biological Evaluation ◽  
Carbonic Anhydrase Ii ◽  
Molecular Docking Studies

scholarly journals Synthesis and Human Carbonic Anhydrase I, II, IX, and XII Inhibition Studies of Sulphonamides Incorporating Mono-, Bi- and Tricyclic Imide Moieties

2021 ◽  
Vol 14 (7) ◽  
pp. 693
Author(s):  
Kalyan K. Sethi ◽  
KM Abha Mishra ◽  
Saurabh M. Verma ◽  
Daniela Vullo ◽  
Fabrizio Carta ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Carbonic Anhydrase ◽  
Docking Studies ◽  
Carbonic Anhydrases ◽  
Molecular Docking Studies ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase ◽  
Inhibition Studies

New derivatives were synthesised by reaction of amino-containing aromatic sulphonamides with mono-, bi-, and tricyclic anhydrides. These sulphonamides were investigated as human carbonic anhydrases (hCAs, EC 4.2.1.1) I, II, IX, and XII inhibitors. hCA I was inhibited with inhibition constants (Kis) ranging from 49 to >10,000 nM. The physiologically dominant hCA II was significantly inhibited by most of the sulphonamide with the Kis ranging between 2.4 and 4515 nM. hCA IX and hCA XII were inhibited by these sulphonamides in the range of 9.7 to 7766 nM and 14 to 316 nM, respectively. The structure–activity relationships (SAR) are rationalised with the help of molecular docking studies.

Probing phenylcarbamoylazinane-1,2,4-triazole amides derivatives as lipoxygenase inhibitors along with cytotoxic, ADME and molecular docking studies

2020 ◽  
pp. 104525
Author(s):  
Saima Muzaffar ◽  
Wardah Shahid ◽  
Naheed Riaz ◽  
Muhammad Saleem ◽  
Muhammad Ashraf ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Docking Studies ◽  
Lipoxygenase Inhibitors ◽  
Molecular Docking Studies

Sulfonamides containing curcumin scaffold: Synthesis, characterization, carbonic anhydrase inhibition and molecular docking studies

2018 ◽  
Vol 76 ◽  
pp. 218-227 ◽  
Author(s):  
Mahmood Ahmed ◽  
Muhammad Abdul Qadir ◽  
Abdul Hameed ◽  
Muhammad Nadeem Arshad ◽  
Abdullah M. Asiri ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Carbonic Anhydrase ◽  
Docking Studies ◽  
Molecular Docking Studies ◽  
Carbonic Anhydrase Inhibition

scholarly journals Recent development of lipoxygenase inhibitors as anti-inflammatory agents

MedChemComm ◽  
2018 ◽  
Vol 9 (2) ◽  
pp. 212-225 ◽  
Author(s):  
Chaoyu Hu ◽  
Shutao Ma
Keyword(s):  
Biological Activity ◽  
Molecular Docking ◽  
Docking Studies ◽  
Lipoxygenase Inhibitors ◽  
Molecular Docking Studies ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Activity Structure ◽  
Recent Developments ◽  
Lox Inhibitors

This review summarizes recent developments of LOX inhibitors. It also contains an introduction to their structures, biological activity, structure–activity relationships and molecular docking studies.

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