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Complex interactions between molecular ions in solution and their effect on protein stability.

Diwakar Shukla1, Curtiss P Schneider, Bernhardt L Trout

  • 1Department of Chemical Engineering, Massachusetts Institute of Technology, E19-502b, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.

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Guanidinium chloride (GdmCl) salt type significantly impacts protein stability. Sulfate salts enhance protein thermostability and reduce aggregation by promoting ion pairing, unlike chloride salts.

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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Protein Science

Background:

  • Protein stability in ionic solutions is governed by protein-ion and ion-ion interactions.
  • Ion-ion interactions are crucial for molecular ions with multiple charged groups.
  • Understanding these interactions is key to controlling protein behavior.

Purpose of the Study:

  • To investigate the influence of homo- and heteroion pairing on protein stability.
  • To use polyarginine salts as a model system to study these effects.
  • To elucidate how intrasolvent interactions can be leveraged to enhance protein stability.

Main Methods:

  • Utilized polyarginine salts as a model system.
  • Analyzed protein thermostability with different salt types (chloride vs. sulfate).
  • Employed molecular dynamics simulations to understand ion-protein interactions.

Main Results:

  • Chloride salts showed decreased thermostability with increasing peptide size, indicating enhanced protein binding.
  • Reduced homoion pairing in chloride salts was linked to aggregation suppression, not denaturation.
  • Sulfate salts exhibited strong heteroion pairing, enhancing thermostability and reducing protein aggregation rates by 10-30 times.

Conclusions:

  • The interplay between homo- and heteroion pairing critically affects protein stability and aggregation.
  • Sulfate counterions can significantly enhance protein stability and reduce aggregation through strong heteroion pairing.
  • This study demonstrates a strategy for leveraging intrasolvent interactions to improve protein stability.