Study Of B-Sheet Helix Interactions Based On ConformationalProperties Of Synthetic D,L-Alternating Decapeptides

Abstract

De novo peptide design is based on the ability to construct peptide sequences with predictable folding patterns. Helices and β-sheet have been the focus of considerable synthetic attentionin attempts to assemble mimics for helical bundles and all β-motifs. In contrast, strategies for construction of β-sheet helix have been less widely explored. The β-sheet helical architecture is constructed from polypeptides that are coiled into a large helix, formed by stacks of β-sheets separated by loops. β-Sheet helices are present in the fibrous form of transyretin, that play an important role in bovine spongiform encephalopathy (BSE) and form the crucial structural elements in insect antifreeze proteins. We report on synthetic analogues able to form β-sheet helices and on the structural comparison with β-helices formed by D,L-alternating peptides.