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Dynamic Structural Changes and Thermodynamics in Phase Separation Processes of an Intrinsically Disordered-Ordered

Steffen Lüdeke1,2, Philipp Lohner2, Lara G Stühn3

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|November 22, 2021
PubMed
Summary

Elastin-like proteins (ELPs) undergo coacervation when a specific number of repeat units adopt a β-turn structure. This conformational threshold is maintained in the assembled polypeptides, impacting protein-based smart materials.

Keywords:
circular dichroismelastin-like proteinsintrinsically disordered proteinsmatrix least-squares global fittingprotein assembly

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Area of Science:

  • Biochemistry
  • Biophysics
  • Materials Science

Background:

  • Elastin-like proteins (ELPs) are crucial biological molecules and models for intrinsically disordered proteins (IDPs).
  • ELPs exhibit dynamic structural transitions linked to coacervates and liquid-liquid phase transitions.
  • The precise conformational state of ELPs below and above coacervation temperature and its role in phase separation remain unclear.

Purpose of the Study:

  • To investigate the conformational changes of ELPs during coacervation.
  • To determine the role of specific conformations in the phase separation of ELPs.
  • To explore the implications for designing protein-based smart materials.

Main Methods:

  • Utilized matrix least-squares global Boltzmann fitting of circular dichroism spectra.
  • Analyzed ELPs with varying repeat units: (VPGVG)20, (VPGVG)40, and (VPGVG)60.
  • Characterized coacervate suspensions using differential scattering.

Main Results:

  • Coacervation was observed to occur sharply at a conformational threshold, approximately 20 repeat units adopting a β-turn structure.
  • The identified β-turn fraction was retained within the assembled polypeptides in the coacervate state.
  • A correlation between conformational status and phase separation was established.

Conclusions:

  • A specific number of repeat units acquiring β-turn conformation acts as a trigger for ELP coacervation.
  • This conformational threshold plays a role in the assembly of ELPs and potentially other protein systems.
  • Findings provide insights for the rational design of advanced protein-based smart materials.