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Polypeptide solvation in water and cyclohexane reveals complex behaviors. Solute polarity, not just hydrophobicity, dictates folding, with the peptide backbone playing a key stabilizing role.

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Area of Science:

  • Biophysics
  • Computational Chemistry
  • Polymer Science

Background:

  • Understanding polypeptide solvation is crucial for protein folding and stability.
  • The interplay between solvent properties (quality, polarity) and polypeptide characteristics (hydrophobicity, chain length) is complex.
  • Existing models often simplify these interactions, necessitating detailed investigations.

Purpose of the Study:

  • To investigate the solvation process of seven polypeptides with varying hydrophobicity and chain length in water and cyclohexane.
  • To elucidate the roles of solvent quality, solvent polarity, and polypeptide intrinsic properties in solvation.
  • To explore non-additivity effects and the contribution of the peptide backbone to polypeptide stability.

Main Methods:

  • Molecular dynamics simulations were employed to model polypeptide behavior.
  • Thermodynamic integration was used to calculate solvation free energies.
  • A range of homopolypeptides (GLY, ALA, ILE, ASN, LYS, ARG, GLU) from tri- to undeca-mers were studied.

Main Results:

  • Undeca-glycine was the only polypeptide to stably collapse in water; others showed folding/unfolding events.
  • All polypeptides maintained extended conformations in cyclohexane, regardless of polarity.
  • Solvation free energies were favorable across all solvent-polypeptide combinations.
  • Solvation was enthalpically dominated for polar polypeptides and entropically driven for hydrophobic ones.

Conclusions:

  • Polypeptide solvation is more complex than the "like dissolves like" principle suggests, with solute polarity being a dominant factor.
  • The peptide backbone significantly stabilizes polypeptides in solution.
  • The study challenges simplistic views of solvation and highlights the importance of detailed molecular simulations.