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<p>We modeled the binding domain of the HIV-1 (human immunodeficiency virus) glycoprotein gp120 (BDgp) in its primary structure composed of amino acids, starting with glycine 365 and ending with valine 430, according to recent research reports, which suggest that HIV entry into human cells requires the interaction of the viral outer envelope glycoprotein, gp120, with the human glycoprotein CD4 (cluster of differentiation 4). The research strategy was the analysis of BDgp by density functional theory (DFT), we identified areas of maximum reactivity, physicochemical properties, and HOMO–LUMO frontier molecular orbitals useful to understand infection and the development of AIDS (acquired immunodeficiency syndrome). We also identified the most reactive and specific amino acids susceptible to gp120 modification, necessary for the design of new pharmacological, therapeutic, and prophylactic strategies.</p> Graphical abstract <p></p>

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Quantum-mechanic analysis of the gp120 glycoprotein of the outer envelope of wild-type HIV-1 necessary to understand infection in AIDS, useful for the development of new pharmacological and therapeutic strategies

  • 期刊论文

  • 发表日期：

    2024年12月31日

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  • Juan Carlos Santiago-Jiménez,
  • Gabriel Ramírez-Damaso,
  • Fray De Landa Castillo-Alvarado

摘要

We modeled the binding domain of the HIV-1 (human immunodeficiency virus) glycoprotein gp120 (BDgp) in its primary structure composed of amino acids, starting with glycine 365 and ending with valine 430, according to recent research reports, which suggest that HIV entry into human cells requires the interaction of the viral outer envelope glycoprotein, gp120, with the human glycoprotein CD4 (cluster of differentiation 4). The research strategy was the analysis of BDgp by density functional theory (DFT), we identified areas of maximum reactivity, physicochemical properties, and HOMO–LUMO frontier molecular orbitals useful to understand infection and the development of AIDS (acquired immunodeficiency syndrome). We also identified the most reactive and specific amino acids susceptible to gp120 modification, necessary for the design of new pharmacological, therapeutic, and prophylactic strategies.

Graphical abstract