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Hydrostatic pressure rescues native protein from aggregates.

D Foguel1, C R Robinson, P C de Sousa

  • 1Departamento de Bioquímica Médica, Instituto de Ciências Biomédicas, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil.

Biotechnology and Bioengineering
|July 9, 1999
PubMed
Summary

Hydrostatic pressure can reverse protein aggregation and increase refolding. This novel method, applied to P22 tailspike protein, dissociates aggregates and promotes native trimer formation without chaotropic agents.

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Area of Science:

  • Biochemistry
  • Biotechnology
  • Structural Biology

Background:

  • Protein misfolding and aggregation are significant challenges in biotechnology, research, and human health.
  • Current refolding methods often require harsh conditions like chaotropic agents or large dilutions.

Purpose of the Study:

  • To introduce a novel method for reversing protein aggregation and enhancing refolding using hydrostatic pressure.
  • To investigate the pressure sensitivity of protein folding and aggregation intermediates.

Main Methods:

  • Utilized P22 tailspike protein as a model system.
  • Identified and quantified aggregation intermediates using size-exclusion high-performance liquid chromatography (HPLC).
  • Applied hydrostatic pressure (2.4 kbar) to protein aggregates.

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Main Results:

  • Hydrostatic pressure treatment dissociated P22 tailspike aggregates.
  • Released pressure led to increased formation of native, active trimers.
  • Refolded trimers were fully active in forming infectious viral particles.

Conclusions:

  • Hydrostatic pressure offers a non-chemical method to reverse protein aggregation and promote refolding.
  • Identified pressure-sensitive intermediates suggest shared recognition determinants in folding and aggregation.
  • This approach can lead to improved protein refolding strategies.