Use of disulfide "staples" to stabilize beta-sheet quaternary structure.

ABSTRACT: 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.

SUBMITTER: Khakshoor O 

PROVIDER: S-EPMC2726807 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature