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Sequence Modulates Polypeptoid Hydration Water Structure and Dynamics.

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Polypeptoid sequence affects surrounding water. More nonpolar groups lead to less dense, more tetrahedral water with slower dynamics, insights confirmed by Overhauser dynamic nuclear polarization (ODNP).

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Area of Science:

  • Polymer Chemistry
  • Computational Chemistry
  • Biophysics

Background:

  • Polypeptoids offer a tunable platform for studying hydration in disordered polymers due to precise sidechain synthesis.
  • Understanding small-molecule hydration within polymers is crucial for various applications, including drug delivery and biomaterials.

Purpose of the Study:

  • To investigate how polypeptoid sequence influences the structure and dynamics of surrounding hydration water.
  • To establish a correlation between water structure and dynamics near polypeptoids.
  • To demonstrate the utility of Overhauser dynamic nuclear polarization (ODNP) in probing site-specific hydration dynamics.

Main Methods:

  • Molecular dynamics (MD) simulations were employed to model water behavior around various peptoid oligomers.
  • A novel computational workflow was utilized for accurate sampling of polypeptoid conformations.
  • Overhauser dynamic nuclear polarization (ODNP) was used to experimentally probe hydration water dynamics.

Main Results:

  • Hydration water exhibited decreased density, increased tetrahedrality, and slower dynamics compared to bulk water.
  • The extent of these changes correlated with the number of nonpolar sidechains in the polypeptoid sequence.
  • A strong correlation was observed between shifts in water structure and dynamics.

Conclusions:

  • Polypeptoid sequence significantly impacts local water properties, with nonpolar groups playing a key role.
  • Experimental measurements of hydration water dynamics, such as via ODNP, can provide insights into water structural properties.
  • ODNP is a valuable technique for site-specific analysis of hydration water dynamics in complex systems.