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HMGB1 B-Box Domain Associates Promote Protein-Polyelectrolyte Interactions.

Marten Kagelmacher1,2, Marina Pigaleva1, Ricardo Zarate1

  • 1Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.

The Journal of Physical Chemistry. B
|September 6, 2025
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Summary
This summary is machine-generated.

High mobility group box 1 (HMGB1) protein self-association, particularly via its B-box domain, enhances heparin binding. This multimerization creates a charged region, improving interactions with polyanions like heparin, crucial for immune regulation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • High mobility group box 1 (HMGB1) is a nuclear protein acting as an extracellular alarmin.
  • HMGB1 signaling can drive inflammation, which is modulated by polyanion binding.
  • HMGB1 undergoes phase separation, linked to its function, potentially involving its B-box domain.

Purpose of the Study:

  • Investigate the role of the HMGB1 B-box domain in protein self-association.
  • Determine how HMGB1 self-association affects its interaction with heparin.
  • Elucidate the structural mechanisms underlying HMGB1-heparin interactions.

Main Methods:

  • Protein self-association analysis of the HMGB1 B-box domain.
  • Electron Paramagnetic Resonance (EPR) spectroscopy to study protein-heparin interactions.
  • AlphaFold modeling to predict structural changes and charge distribution.

Main Results:

  • The HMGB1 B-box domain forms stable 30 nm self-associates.
  • Protein associates significantly enhance heparin binding compared to individual chains.
  • AlphaFold modeling revealed that multimerization creates an extended positive charge region enhancing polyanion binding.

Conclusions:

  • HMGB1 self-association, mediated by the B-box domain, is critical for enhanced heparin binding.
  • Multimerization-induced charge redistribution explains increased affinity for polyanions like heparin.
  • These findings provide structural insights into HMGB1's role in immune modulation and phase separation.