Use of disulfide "staples" to stabilize beta-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.
Khakshoor
Omid
O
Department of Chemistry, University of California, Irvine, Irvine, California 92697-2025, USA.
Nowick
James S
JS
D004151:Dipeptides / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry*; D006860:Hydrogen Bonding; D015394:Molecular Structure; D010456:Peptides, Cyclic / Q000737:chemistry*; D017433:Protein Structure, Secondary / Q000187:drug effects*; D014867:Water / Q000737:chemistry
D004151:Dipeptides; D004220:Disulfides; D010456:Peptides, Cyclic; D014867:Water; C046557:cysteinylcysteine