<i>In silico</i> approach revealed the membrane receptor PHO36 as a new target for synthetic anticandidal peptides

<b>Aim:</b> Synthetic antimicrobial peptides (SAMPs) present the potential to fight systemic fungal infections. Here, the PHO36 receptor from <i>Candida albicans</i> was analyzed by <i>in silico</i> tools as a possible target for three anticandidal SAMPs: <i>Rc</i>Alb-PepIII, PepGAT and PepKAA. <b>Materials &amp; methods:</b> Molecular docking, dynamics and quantum biochemistry were employed to understand the individual contribution of amino acid residues in the interaction region. <b>Results:</b> The results revealed that SAMPs strongly interact with the PHO36 by multiple high-energy interactions. This is the first study to employ quantum biochemistry to describe the interactions between SAMPs and the PHO36 receptor. <b>Conclusion:</b> This work contributes to understanding and identifying new molecular targets with medical importance that could be used to discover new drugs against systemic fungal infections. Here, computers helped us find new proteins in <i>Candida albicans</i> that may guide the development of new medicines. This is the first work to study by quantum biochemistry calculation of the interaction of SAMPs with the receptor PHO36. Molecular docking and dynamics simulation revealed the complex formation and stabilization between SAMPs and PHO36. Quantum biochemistry calculations revealed the amino acid residues with attractive and repulsive forces in the complexes’ formation. Quantum biochemistry analysis revealed a high global interaction energy between peptides and PHO36.