Disulfide-based beta-sheet peptidomimetics

CHED 561

Timothy J. Cashman and Brian R. Linton, blinton@bowdoin.edu. Department of Chemistry, Bowdoin College, 6600 College Station, Brunswick, ME 04011
Small molecules that resemble beta-sheets may be capable of mimicking the behavior of naturally occurring beta-sheets without the added complexity of the protein in its entirety. These small molecules have become important tools in understanding molecular recognition, protein-protein interactions and protein folding. A cystine dimer is a simple and easily created molecule that exhibits such a structure. The disulfide bond between the cystines functions as an effective scaffold for hydrogen bond formation that is consistent with beta-sheet secondary structure. Extension of the peptide strands to increase the number of hydrogen bonds produces a structure that more closely resembles naturally occurring beta-sheets.