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Entropic stabilization of isolated beta-sheets.

Philippe Dugourd¹, Rodolphe Antoine, Gary Breaux

¹Laboratoire de Spectrométrie Ionique et Moléculaire, UMR No. 5579, CNRS et Université Lyon 1, 43 bd du 11 novembre 1918, 69622 Villeurbanne Cedex, France.

Journal of the American Chemical Society

|March 31, 2005

Summary

Unsolvated alanine-based peptides (Ac-WA(n)-NH(2)) with more than 10 alanine units adopt beta-sheet structures at room temperature. Peptide structure in the gas phase is primarily controlled by charge location, not alanine

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Area of Science:

Biophysics
Computational Chemistry
Peptide Science

Background:

Alanine-based peptides are fundamental models in biophysical studies.
Peptide conformation in solution differs significantly from gas-phase or solid-state structures.
Previous research indicates charge location influences gas-phase peptide structures.

Purpose of the Study:

To investigate the gas-phase conformations of unsolvated alanine-based peptides.
To determine the influence of peptide length and charge on secondary structure.
To compare solution-phase and gas-phase structural propensities of alanine-rich sequences.

Main Methods:

Temperature-dependent electric deflection measurements were used to probe peptide structures.
Monte Carlo simulations with a parallel tempering algorithm were employed for data interpretation.
A series of acetylated tryptophan-alanine peptides (Ac-WA(n)-NH(2)) with varying alanine lengths (n=3, 5, 10, 13, 15) were studied.

Main Results:

Unsolvated Ac-WA(n)-NH(2) peptides with n > 10 predominantly adopt beta-sheet conformations at room temperature.
This contrasts with the high helix propensity of alanine in solution.
Peptide structure is highly sensitive to the location of the charge, as previously observed.

Conclusions:

Gas-phase secondary structures of alanine-based peptides are not solely dictated by intrinsic amino acid propensities.
Peptide length and the absence of solvent play crucial roles in determining stable conformations.
Charge localization is the dominant factor governing the overall structure of these peptides in the gas phase.