Nanomolar Sensitivity Chirality Transfer from Designed Helical Repeat Proteins to Achiral CdS Nanorods

Bridging chirality across length scales with inorganic-organic hybrid materials is a rapidly expanding area of research. Here, we establish asymmetry at CdS nanorod (NR) interfaces using a designed helical repeat protein bearing four cysteine residues (DHR-4Cys). Hydrophobic NRs are transferred into water with glycine, and then glycine is displaced by DHR-4Cys, leveraging the thiophilicity of cadmium. Circular dichroism (CD) in the visible, coincident with CdS electronic transitions, reveals a chiral DHR-4Cys:CdS interface. The dissymmetry factor [<i>g</i>-factor = 4.5 × 10^-4 (short NRs) and 5.0 × 10^-4 (long NRs)] is weakly dependent on the NR length, and CD persists at nanomolar protein loadings. Additionally, control experiments demonstrate that DHR-4Cys:CdS NR chirality is dictated by the local coordination of Cys with no significant contribution from the chiral secondary structure of the protein (<i>g</i>-factors of short and long Cys:CdS NRs are 4.8 × 10^-4 and 4.0 × 10^-4, respectively). Together with far-UV CD and transmission electron microscopy, which provide evidence of preserved protein structure, these results provide the first demonstration that a structurally defined protein can induce chirality in CdS nanocrystals while maintaining protein structure at biologically relevant concentrations.