Discovery of Novel Sulfonamide‐Based 5‐Arylidenerhodanines as Effective Carbonic Anhydrase (II) Inhibitors: Microwave‐Assisted and Ultrasound‐Assisted One‐Pot Four‐Component Synthesis, Molecular Docking, and Anti‐CA II Screening Studies

2019 ◽  
Vol 56 (9) ◽  
pp. 2460-2468 ◽  
Author(s):  
Arif Mermer ◽  
Neslihan Demirbas ◽  
Ummuhan Cakmak ◽  
Ahmet Colak ◽  
Ahmet Demirbas ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Ii ◽  
One Pot ◽  
Microwave Assisted ◽  
Ultrasound Assisted

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.

One‐pot, Four‐Component Green Synthesis, Carbonic Anhydrase II Inhibition and Docking Studies of 5‐Arylidenerhodanines

2018 ◽  
Vol 3 (43) ◽  
pp. 12234-12242 ◽  
Author(s):  
Arif Mermer ◽  
Neslihan Demirbas ◽  
Ahmet Colak ◽  
Elif Ayazoglu Demir ◽  
Necla Kulabas ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Green Synthesis ◽  
Docking Studies ◽  
Carbonic Anhydrase Ii ◽  
One Pot

scholarly journals Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance

Catalysts ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 401
Author(s):  
Mengzhao Jiao ◽  
Jie He ◽  
Shanshan Sun ◽  
Frank Vriesekoop ◽  
Qipeng Yuan ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
High Efficiency ◽  
Specific Binding ◽  
Metal Organic Framework ◽  
Immobilized Enzymes ◽  
Catalytic Performance ◽  
Carbonic Anhydrase Ii ◽  
One Pot ◽  
Original Activity ◽  
Simple Strategy

Carbonic anhydrase (CA) has received considerable attention for its ability to capture carbon dioxide efficiently. This study reports a simple strategy for immobilizing recombinant carbonic anhydrase II from human (hCA II) on Ni-based MOFs (Ni-BTC) nanorods, which was readily achieved in a one-pot immobilization of His-tagged hCA II (His-hCA II). Consequently, His-hCA II from cell lysate could obtain an activity recovery of 99% under optimal conditions. After storing for 10 days, the immobilized His-hCA II maintained 40% activity while the free enzyme lost 91% activity. Furthermore, during the hydrolysis of p-nitrophenyl acetic acid, immobilized His-hCA II exhibited excellent reusability and still retained more than 65% of the original activity after eight cycles. In addition, we also found that Ni-BTC had no fixation effect on proteins without histidine-tag. These results show that the Ni-BTC MOFs have a great potential with high efficiency for and specific binding of immobilized enzymes.

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