Design of Highly Stabilized β-Hairpin Peptides through Cation−π Interactions of Lysine and N-Methyllysine with an Aromatic Pocket
- 3 February 2009
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 48 (7) , 1525-1531
- https://doi.org/10.1021/bi801706k
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.Keywords
This publication has 32 references indexed in Scilit:
- Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effectProceedings of the National Academy of Sciences, 2007
- Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURFNature, 2006
- The diverse functions of histone lysine methylationNature Reviews Molecular Cell Biology, 2005
- Comparison of C−H···π and Hydrophobic Interactions in a β-Hairpin Peptide: Impact on Stability and SpecificityJournal of the American Chemical Society, 2004
- The geometry and efficacy of cation–π interactions in a diagonal position of a designed β‐hairpinProtein Science, 2003
- Design of Non-Cysteine-Containing Antimicrobial β-Hairpins: Structure−Activity Relationship Studies with Linear Protegrin-1 AnaloguesBiochemistry, 2002
- Effects of Amino Acid φ,ψ Propensities and Secondary Structure Interactions in Modulating Hα Chemical Shifts in Peptide and Protein β-SheetJournal of the American Chemical Society, 2001
- A Minimal Peptide Scaffold for β-Turn Display: Optimizing a Strand Position in Disulfide-Cyclized β-HairpinsJournal of the American Chemical Society, 2000
- Dissecting the stability of a β-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the β-turn and β-strand contributions to folding 1 1Edited by P. E. WrightJournal of Molecular Biology, 1999
- The Cation−π InteractionChemical Reviews, 1997