Quantum Mechanical Study of Interaction between Phenolic Compounds as Inhibitor with Active Site of Human Carbonic Aanhydrase (II) Enzyme

Publish Year: 1397
نوع سند: مقاله کنفرانسی
زبان: English
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ISPTC21_065

تاریخ نمایه سازی: 30 دی 1397

Abstract:

CO2, bicarbonate and protons are an essential molecule and ions for many importantphysiologic processes occurring in all living organisms. However, the uncatalyzed rate ofinterconversion of such species is too slow to meet the physiological needs of most biochemicalprocesses. This task is efficiently accomplished by the carbonic anhydrases. This superfamily ofmetals-enzymes prossess within their active sites a highly nucleophilic metal hydroxide species,such as zinc(II), cadmium(II) or iron (II) hydroxide, depending on the class [1].Phenol and its derivatives were reported to be a competitive of human CarbonicAnhydrase II (hCA II). The phenolic moiety has an amphiphilic character. The presence of thehydrophobic planar aromatic ring is responsible for hydrophobic interactions (π-stacking),whereas at the same time the polar hydroxyl groups can participate in hydrogen bonding. Thisdual behavior allows these molecules to bind to the amino acid residues of several proteins,enzymes or receptors [2]. In the present research the mechanism of the inhibition of phenoliccompounds with active form of CA (II) using DFT calculations have been investigated. Theelectronic structure and electronic energy of all studied compounds have been calculated in thegas phase and then in water solvent using B3LYP and split-valance6-31G* basis set.

Authors

Nasrin Emami Golia

Vanak Village Street, Alzahra university, Tehran Province, Tehran

Mina Ghiasib

Vanak Village Street, Alzahra university, Tehran Province, Tehran