Noble metals have garnered significant attention as broad‐spectrum antiviral materials for decades, particularly following the SARS‐CoV‐2 pandemic in 2019. Noble metal‐composited materials feature great advantages such as high biocompatibility, low toxicity, and remarkable durability, making them ideal candidates for antiviral applications. However, the atomic‐level understanding of the metal–protein interactions is still unclear, requiring insights from both experimental and theoretical aspects. In this study, we employ density functional theory calculations to investigate the interactions between SARS‐CoV‐2 Spike protein fragments and noble metal (Au/Ag) surfaces regarding their electronic structures and configurational characteristics. It is found that the inherent features of surface metals and functional groups on the protein fragments are essential factors influencing the contact phenomena. Furthermore, interfacial contact orientation and area significantly influence binding affinity and bond formation processes. We also verify the potential self‐adsorption‐induced configurational changes through the structural variations and the isosurface projection of electronic distributions. These results suggest that Au/Ag sufficiently disrupts the natural protein conformations and electronic characteristics, which highlights their potential as robust antiviral materials for air filtering systems and disinfectant materials.
Lu et al. (Sun,) studied this question.