Stereodivergent Chirality Transfer by Noncovalent Control of Disulfide Bonds

Controlling dynamic
stereochemistry is an important challenge,
as it is not only inherent to protein structure and function but often
governs supramolecular systems and self-assembly. Typically, disulfide
bonds exhibit stereodivergent behavior in proteins; however, how chiral
information is transmitted to disulfide bonds remains unclear. Here,
we report that hydrogen bonds are essential in the control of disulfide
chirality and enable stereodivergent chirality transfer. The formation
of S–S···H–N hydrogen bonds in solution
can drive conformational adaption to allow intramolecular chirality
transfer, while the formation of C=O···H–N hydrogen
bonds results in supramolecular chirality transfer to form antiparallel
helically self-assembled solid-state architectures. The dependence
on the structural information encoded in the homochiral amino acid
building blocks reveals the remarkable dynamic stereochemical space
accessible through noncovalent chirality transmission.