Abstract
The synthesis and utilization of novel thiostatines (β-SH-substituted γ-amino acids) in the design of backbone-disulfide-stabilized β-hairpin mimetics, solution conformations of hybrid β-hairpins and Cys-disulfide-stabilized α-peptide analogue, their thiol exchange, and proteolytic stability are investigated. The results suggest that thiostatines can be used to design proteolytically stable water-soluble β-hairpin mimetics without deviating from overall β-hairpin conformation.
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