Effect of supramolecular chirality on nano-protein/cell interaction: An experimental and computational investigation
Understanding the unique role of supramolecular chirality in nano-protein/cell interactions, as opposed to molecular chirality, is crucial for elucidating the origin of life. However, this aspect has received inadequate attention. In this study, L/D-glutamic acid-based amphiphiles (L/D-GluC16), which possess molecular chirality, were synthesized. Additionally, through the manipulation of solvent effects, left/right-handed helical nanofibers ( M / P -GluC16), endowed with supramolecular chirality, were assembled from L/D-GluC16. With the aid of molecular dynamics (MD) simulations, the interaction between M / P -GluC16, L/D-GluC16, and a model protein (bovine serum albumin, BSA) was investigated at the thermodynamic and spatial orientational levels. Combined with the experimental result of protein adsorption efficiency, a more favorable chirality-dependent binding of M / P -GluC16 to protein compared to L/D-GluC16 was confirmed. Furthermore, driven by the binding-induced conformational changes and subsequent functional disruptions of proteins, M / P -GluC16 exhibited a greater chirality-specific cancer cell inhibitory efficacy compared to L/D-GluC16, highlighting the more significant impact of supramolecular chirality on nano-protein/cell interactions than molecular chirality.
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