Abstract
Chiral communications exist in secondary structures of foldamers and copolymers via a network of noncovalent interactions within effective intermolecular force (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 (<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 peptide domains. Our findings establish that long-range chiral transmission occurs in tertiary macromolecular domains, explaining the presence of homochiral pairing of superhelices in proteins.
Highlights
Chiral communications exist in secondary structures of foldamers and copolymers via a network of noncovalent interactions within effective intermolecular force (IMF) range
It remains elusive whether chiral-to-chiral communication is permitted beyond the IMF distance between higher-order macromolecular domains such as peptide tertiary structures
These findings indicated that chiral communications are present in the secondary structures of copolymers and non-proteogenic peptides, and exist between two biomacromolecular domains in a long-range manner (
Summary
Chiral communications exist in secondary structures of foldamers and copolymers via a network of noncovalent interactions within effective intermolecular force (IMF) range. The interaction strength is determined by an ensemble set of intermolecular forces (IMF) between functional groups, which is effective on the length scale of Van der Waals radius[23] It remains elusive whether chiral-to-chiral communication is permitted beyond the IMF distance between higher-order macromolecular domains such as peptide tertiary structures. The three interdomain linkers adopted restricted conformations via hydrophobic interactions, which likely explained the chiral conduction between the trimeric peptide coiled-coil and the DNA triplex These findings indicated that chiral communications are present in the secondary structures of copolymers and non-proteogenic peptides, and exist between two biomacromolecular domains in a long-range manner (
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