Docking of sulfonamides to carbonic anhydrase II and IV

Esposito, Emilio Xavier; Baran, Kelli; Kelly, K.; Madura, Jeffry D.

doi:10.1016/s1093-3263(00)00040-1

Cited by 44 publications

(21 citation statements)

References 35 publications

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“…These docking calculations demonstrate that MOE‐Dock can successfully reproduce the crystal structures of different RT/inhibitor complexes, consistent with the calculations of carbonic anhydrase II and IV complexes by Esposito et al41, 42 Hence, MOE‐Dock was used to explore potential binding positions in the RT active site as well as interactions with the protein for several new RT diterpenoid inhibitors (Fig. 2).…”

Section: Resultssupporting

confidence: 82%

Docking of non‐nucleoside inhibitors: Neotripterifordin and its derivatives to HIV‐1 reverse transcriptase

2002

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The docking of small molecules to proteins has played an important role in the understanding of drug/receptor interactions. An important drug/receptor interaction is between non-nucleoside inhibitors of HIV-1 RT and the non-nucleoside binding pocket. We report the results of docking calculations in which we have docked known and proposed non-nucleoside reverse transcriptase inhibitors to the type 1 virus. The proposed NNRTIs dock in a similar position and orientation as known inhibitors. In addition, we observe a linear correlation between the calculated interaction energy and EC50 for the inhibitors, suggesting that the docked structure orientation and the interaction energies are reasonable. Two hydrogen bonds between nevirapine and RT (3HVT and 1VRT) are observed and are reproduced across different docking schemes. Since we used two different HIV-1 RT crystal structures (3HVT and 1VRT), which are at different levels of resolution (2.9 and 2.2 A, respectively), we propose that structures with resolutions better than 3 A can be used to produce reasonable docking results.

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Section: Resultssupporting

confidence: 82%

Docking of non‐nucleoside inhibitors: Neotripterifordin and its derivatives to HIV‐1 reverse transcriptase

2002

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“…These results indicated that vitamin E entered the erythrocytes and inhibition of CA activity may have occurred through direct binding to the functional group of CA or by displacing the metal associated with the enzyme as has been reported previously by some researchers (Lindskog, 1997;Briganti et al, 1998;Esposito et al, 2000). Thus, in vivo studies on vitamin E supported the results of in vitro studies.…”

Section: Discussionsupporting

confidence: 84%

Effect of vitamin E on carbonic anhydrase enzyme activity in rainbow trout (Oncorhynchus mykiss) erythrocytes in vitro and in vivo

Aras-Hisar

Hisar

Beydemır

et al. 2004

Acta Veterinaria Hungarica

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Considering that the excessive usage of vitamin E causes hypervitaminosis and thus reduces blood erythrocyte concentrations, therefore it is worth studying how its pharmacological dosage affects the activity of carbonic anhydrase (CA) enzyme found in erythrocytes of rainbow trout (Oncorhynchus mykiss) in vitro and in vivo. Vitamin E inhibited CA enzyme and the IC 50 value of the vitamin was 0.039 mM in vitro. Similarly, it was seen that vitamin E inhibited CA enzyme activity after the first hour following vitamin E injections in vivo. The activities of CA in groups of trout given vitamin E injection were measured at 1, 3 and 5 h and the corresponding activities were found to be 772.7 ± 290.5 (P < 0.05), 1286.4 ± 378.2 and 1005.7 ± 436.1 enzyme units (EU) g Hb -1 . The difference over the control was significant (P < 0.05) in the first hour and insignificant at 3 and 5 h (P > 0.05). The activity of CA in the control, which did not contain vitamin E, was determined as 1597.7 ± 429.0 EU g Hb -1 .

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“…The 3D structure of STSA for all sequence alignments was generated by homology modeling as a template of the X-ray crystal structure (PDB ID: 2SIM) using the Molecular Operating Environment (MOE) program package (MOE 2011.10, Chemical Computing Group, Montreal, QC, Canada) [ 19 ]. Docking simulations of Neu5Ac2en or Neu5Gc2en to the STSA structure were carried out by the MOE-Dock method [ 20 ]. The binding affinity was evaluated using the correlated fragment molecular orbital (FMO) calculations at the RI-MP2 / cc-pVDZ level [ 21 ].…”

Section: In Silico Analysismentioning

confidence: 99%

Catalytic preference of Salmonella typhimurium LT2 sialidase for N‐acetylneuraminic acid residues over N‐glycolylneuraminic acid residues

et al. 2013

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In a comparison of sialidase activities toward N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc), we found that Salmonella typhimurium LT2 sialidase (STSA) hardly cleaved 4-methylumbelliferyl Neu5Gc (4MU-Neu5Gc). The kcat/Km value of STSA for 4MU-Neu5Gc was found to be 110 times lower than that for 4-methylumbelliferyl Neu5Ac (4MU-Neu5Ac). Additionally, STSA had remarkably weak ability to cleave α2-3-linked-Neu5Gc contained in gangliosides and equine erythrocytes. In silico analysis based on first-principle calculations with transition-state analogues suggested that the binding affinity of Neu5Gc2en is 14.3 kcal/mol more unstable than that of Neu5Ac2en. The results indicated that STSA preferentially cleaves Neu5Ac residues rather than Neu5Gc residues, which is important for anyone using this enzyme to cleave α2-3-linked sialic acids.

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Docking of sulfonamides to carbonic anhydrase II and IV

Cited by 44 publications

References 35 publications

Docking of non‐nucleoside inhibitors: Neotripterifordin and its derivatives to HIV‐1 reverse transcriptase

Docking of non‐nucleoside inhibitors: Neotripterifordin and its derivatives to HIV‐1 reverse transcriptase

Effect of vitamin E on carbonic anhydrase enzyme activity in rainbow trout (Oncorhynchus mykiss) erythrocytes in vitro and in vivo

Catalytic preference of Salmonella typhimurium LT2 sialidase for N‐acetylneuraminic acid residues over N‐glycolylneuraminic acid residues

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