PubReading [151] - Chirality transmission in macromolecular domains - S. Pandey, C. Lou, H.Mao et al

<p><strong>Chiral communications</strong> exist in secondary structures of <strong>foldamers</strong> and <strong>copolymers</strong> via a network of noncovalent interactions within effective <strong>intermolecular force</strong> (IMF) range. It is not known whether long-range chiral communication exists between macromolecular tertiary structures such as peptide coiled-coils beyond the IMF distance. Harnessing the high sensitivity of single-molecule force spectroscopy, we investigate the chiral interaction between covalently linked DNA duplexes and peptide coiled-coils by evaluating the binding of a diastereomeric pair of three DNA-peptide conjugates. We find that right-handed DNA triple helices well accommodate peptide triple coiled-coils of the same handedness, but not with the left-handed coiled-coil stereoisomers. This chiral communication is effective in a range (&lt;4.5 nm) far beyond canonical IMF distance. Small-angle X-ray scattering and molecular dynamics simulation indicate that the interdomain linkers are tightly packed via hydrophobic interactions, which likely sustains the chirality transmission between DNA and <strong>peptide</strong> domains. Our findings establish that long-range chiral transmission occurs in tertiary macromolecular domains, explaining the presence of homochiral pairing of superhelices in proteins.</p><p><em>doi.org/10.1038/s41467-021-27708-4 - 2022</em></p>