The non-covalent stereocontrol of disulfide bonds
Titouan Chetot1, Adrien Forot1,2, Elise Dumont3
1CNRS, Univ. Claude Bernard Lyon 1, ICBMS, UMR5246, F-69622 Villeurbanne, France.
Abstract:
Disulfide bonds are pivotal in shaping the structure and function of both natural proteins and synthetic architectures, yet the stereochemical control of their axial chirality has only very recently garnered focused attention. In this review, we have (re)-examined the published structures of natural and synthetic disulfide-containing compounds to uncover the non-covalent interactions that can bias the chirality of the S-S bond toward specific P or M conformations. Building on these insights, we provide here a conceptual toolbox that could inspire various communities, from molecular biologists exploring the role of disulfide bridges in transmitting stereochemical information within protein structures to organic chemists designing disulfide-based architectures of increased complexity.
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