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Polymorphism of Lysozyme Condensates.

Mohammad S Safari1, Michael C Byington1, Jacinta C Conrad1

  • 1Department of Chemical and Biomolecular Engineering, University of Houston , 4726 Calhoun Road, Houston, Texas 77204-4004, United States.

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This summary is machine-generated.

Mesoscopic protein clusters, distinct from amyloid structures, are identified as precursors to ordered protein solids. Their limited size and retained enzymatic activity suggest protein conformational stability controls condensation pathways.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Structural Biology

Background:

  • Protein condensates are vital in biological processes and diseases.
  • Mesoscopic protein clusters may precede ordered protein solid formation (e.g., amyloid fibrils).
  • These clusters exhibit characteristics of both native and misfolded proteins, challenging existing models.

Purpose of the Study:

  • To differentiate mesoscopic protein clusters from amyloid structures and disordered aggregates.
  • To investigate the properties and formation mechanisms of these distinct protein aggregates.
  • To explore the role of protein conformational stability in protein condensation pathways.

Main Methods:

  • Utilized the antimicrobial enzyme lysozyme for experimental analysis.
  • Compared mesoscopic clusters with amyloid structures and chemically modified disordered aggregates.
  • Assessed cluster size, reversibility, and retained enzymatic activity.

Main Results:

  • Mesoscopic clusters are distinct from amyloid and disordered aggregates.
  • Cluster formation and amyloid oligomerization are reversible; S-S bond reduction-induced aggregation is permanent.
  • Protein molecules within clusters retain enzymatic activity, unlike in amyloid structures.
  • Mesoscopic clusters have a constant radius (<50 nm), while other aggregates grow rapidly.

Conclusions:

  • Mesoscopic clusters result from limited protein structural flexibility.
  • Controlling protein conformational stability can direct protein condensation pathways.
  • These findings offer insights into the nucleation of ordered protein solids.