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Article

Design of Highly Stabilized β-Hairpin Peptides through Cation−π Interactions of Lysine and N-Methyllysine with an Aromatic Pocket^†

Supporting Info

Alexander J. Riemen and Marcey L. Waters*

Department of Chemistry, CB 3290, University of North Carolina, Chapel Hill, North Carolina 27599

Biochemistry, 2009, 48 (7), pp 1525–1531

DOI: 10.1021/bi801706k

Publication Date (Web): February 3, 2009

†

This research was supported by a grant from the National Institutes of Health (1R01 GM071589).

, * To whom correspondence should be addressed. Phone: (919) 843-6522. Fax: (919) 923-6344. E-mail: mlwaters@email.unc.edu.

Abstract

Two tryptophan residues were incorporated on one face of a β-hairpin peptide to form an aromatic pocket that interacts with a lysine or N-methylated lysine via cation−π interactions. The two tryptophan residues were found to pack against the lysine side chain forming an aromatic pocket similar to those observed in trimethylated lysine receptor proteins. Thermal analysis of methylated lysine variant hairpin peptides revealed an increase in thermal stability as the degree of methylation was increased, resulting in the most thermally stable β-hairpin reported to date.

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History

Published In Issue February 24, 2009
Article ASAPFebruary 03, 2009
Received: September 08, 2008
Revised: December 05, 2008

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Article

Design of Highly Stabilized β-Hairpin Peptides through Cation−π Interactions of Lysine and N-Methyllysine with an Aromatic Pocket^†