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Stabilizing capping motif for β-hairpins and sheets
Brandon L. Kier, Irene Shu, Lisa A. Eidenschink, Niels H. Andersen and William F. DeGrado
Proceedings of the National Academy of Sciences of the United States of America
Vol. 107, No. 23 (June 8, 2010), pp. 10466-10471
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/25681806
Page Count: 6
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Although much has been learned about the design of models of β-sheets during the last decade, modest fold stabilities in water and terminal fraying remain a feature of most β-hairpin peptides. In the case of hairpin capping, nature did not provide guidance for solving the problem. Some observations from prior turn capping designs, with further optimization, have provided a generally applicable, "unnatural" beta cap motif (alkanoyl-Trp at the N terminus and Trp-Thr-Gly at the C terminus) that provides a net contribution of 6+ kJ/mol to β-hairpin stability, surpassing all other interactions that stabilize β-hairpins including the covalent disulfide bond. The motif, made up entirely of natural residues, is specific to the termini of antiparallel β-strands and reduces fraying at the ends of hairpins and other β-sheet models. Utilizing this motif, 10- to 22-residue peptide scaffolds of defined stereochemistry that are greater than 98% folded in water have been prepared. The β-cap can also be used to staple together short antiparallel β-strands connected by a long flexible loop.
Proceedings of the National Academy of Sciences of the United States of America © 2010 National Academy of Sciences