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Selective aromatic interactions in beta-hairpin peptides.

Chad D Tatko¹, Marcey L Waters

¹Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290, USA.

Journal of the American Chemical Society

|August 9, 2002

Summary

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Phenylalanine (Phe) residues prefer to interact with themselves in peptide structures, offering greater stability than cyclohexylalanine (Cha) interactions. This self-association preference stems from unique aromatic interactions in water.

Area of Science:

Biochemistry
Biophysics
Structural Biology

Background:

Hydrophobic interactions are crucial for protein folding and stability.
Understanding residue-specific interactions within peptides informs protein structure prediction.

Purpose of the Study:

To investigate the selectivity of hydrophobic cluster formation in peptides.
To compare cross-strand interactions of phenylalanine (Phe) and cyclohexylalanine (Cha) in a beta-hairpin.

Main Methods:

Utilized a beta-hairpin peptide model system.
Employed Nuclear Magnetic Resonance (NMR) spectroscopy to analyze interactions.
Performed thermodynamic analysis (enthalpic and entropic values).

Main Results:

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Observed a preference for phenylalanine (Phe) self-association over cyclohexylalanine (Cha) self-association.
Quantified a stability contribution of 0.55 kcal/mol for Phe-Phe pairs relative to Cha-Cha pairs.
NMR data revealed edge-face interaction geometry for Phe-Phe pairs, even when solvent-exposed.

Conclusions:

Aromatic residues like Phe exhibit inherent preferences for self-association in hydrophobic clusters.
Differences in the nature of aromatic versus aliphatic interactions in water drive this selectivity.
Findings contribute to understanding the principles governing peptide and protein structure stabilization.