Use of Disulfide Staples To Stabilize β-Sheet Quaternary Structure

This Letter reports the use of disulfide linkages to stabilize a beta-sheet dimer with a well-defined structure in aqueous and dimethyl sulfoxide solutions. In this dimer, two cyclic beta-sheet peptides are connected by disulfide linkages at the non-hydrogen-bonded rings. The cyclic,beta-sheet domains interact through hydrogen bonding to form a four-stranded beta-sheet structure. This interaction results in enhanced folding of the cyclic beta-sheet peptides.