Online Journal of Microbiological Research

Volume 2, Number 1, 2022

Open Access September 20, 2022 Endnote/Zotero/Mendeley (RIS) BibTeX

Drug-Receptor Interaction of Peptidic HIV-1 Protease: Polar Effect-II

Online Journal of Microbiological Research 2022, 2(1), 1-11. DOI: 10.31586/ojmr.2022.414
Abstract
Klopman described the chemical reaction of metal ions and base ions in term of softness, En and Em, respectively. By simple modification of known methods, Singh et al. made it applicable for neutral Lewis acids (transition metal salts) and bases (organic molecules) and also extended its application to biological systems
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Klopman described the chemical reaction of metal ions and base ions in term of softness, En and Em, respectively. By simple modification of known methods, Singh et al. made it applicable for neutral Lewis acids (transition metal salts) and bases (organic molecules) and also extended its application to biological systems for site selectivity and to explain reaction mechanism (markovnikov and anti-markovnikov rule), ligand-receptor interaction of testosterones, estrogens and tetrahydroimidazobenzodiazepinone. In this study effective atomic softness En(eff) and Em(eff), and their change ΔEnm have been used for site selectivity and polar interaction between 51 peptidic HIV-1 protease inhibitors and receptor amino acids. ΔEnm values derived from drug-receptor interaction show that when one moiety on receptor behaves as nucleophile (O of valine amino acid) at the same time maximum electrophilic site of the drug (C-atom of the maximum En(eff) value) orient itself to come close the respective site and make maximum interaction, while when another moiety on receptor behaves as electrophilic site (C of isoleucine amino acid), at the same time maximum nucleophilic site of the drug (O-atom of the maximum Em(eff) value) also orient itself to come close the respective site and make maximum interaction.Full article
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ISSN: 2833-9711
DOI prefix: 10.31586/ojmr
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