Reversible Dimerization of Human Serum Albumin

Alexey Chubarov, Anna Spitsyna, Olesya Krumkacheva, Dmitry Mitin, Daniil Suvorov, Victor Tormyshev, Matvey Fedin, Michael K. Bowman, Elena Bagryanskaya

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

Pulsed Dipolar Spectroscopy (PDS) methods of Electron Paramagnetic Resonance (EPR) were used to detect and characterize reversible non-covalent dimers of Human Serum Albumin (HSA), the most abundant protein in human plasma. The spin labels, MTSL and OX063, were attached to Cys-34 and these chemical modifications of Cys-34 did affect the dimerization of HSA, indicating that other post-translational modifications can modulate dimer formation. At physiologically relevant concentrations, HSA does form weak, non-covalent dimers with a well-defined structure. Dimer formation is readily reversible into monomers. Dimerization is very relevant to the role of HSA in the transport, binding, and other physiological processes.

Original languageEnglish
Article number108
Number of pages12
JournalMolecules (Basel, Switzerland)
Volume26
Issue number1
DOIs
Publication statusPublished - Jan 2021

Keywords

  • aggregation
  • human serum albumin
  • pulse dipole EPR
  • DIMER
  • DYNAMICS
  • BINDING

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