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Metallocomplex-Peptide Interactions Studied by Ultrahigh Resolution Mass Spectrometry.

Cookson K C Chiu1, Yuko P Y Lam1, Christopher A Wootton1

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Journal of the American Society for Mass Spectrometry
|January 23, 2020
PubMed
Summary

This study reveals that the organo-osmium anticancer complex Os1-Cl binds to multiple sites on bovine serum albumin (BSA). Electron capture dissociation mass spectrometry (ECD MS/MS) successfully identified lysine as a novel binding site, alongside known targets.

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Area of Science:

  • Organometallic Chemistry
  • Biochemistry
  • Analytical Chemistry

Background:

  • Organo-osmium complexes, such as OsII arene anticancer complex [(η6-bip)Os(en)Cl]+ (Os1-Cl), exhibit strong binding to DNA and biomolecules.
  • Understanding the interaction of these complexes with proteins is crucial for their development as therapeutic agents.

Purpose of the Study:

  • To investigate the binding interaction between the Os1-Cl complex and bovine serum albumin (BSA), a model protein.
  • To determine the specific binding locations of Os1-Cl on BSA using advanced mass spectrometry techniques.

Main Methods:

  • Ultrahigh resolution Fourier transform-ion cyclotron resonance mass spectrometry (FT-ICR MS) was employed to analyze the Os1-Cl-BSA interaction.
  • Collisionally activated dissociation (CAD) and electron capture dissociation (ECD) MS/MS techniques were used to localize the osmium modification.
  • Nano liquid chromatography (nLC)-FT-ICR ECD MS/MS was utilized for comprehensive mapping of binding sites.

Main Results:

  • Collisionally activated dissociation (CAD) MS/MS readily dissociated the osmium complex, losing location information.
  • Electron capture dissociation (ECD) MS/MS successfully retained the osmium modification on peptides, enabling localization.
  • Lysine was identified as a novel binding site for Os1-Cl, in addition to expected sites like methionine, histidine, and cysteine. Multiple binding locations were revealed, including N- and C-termini, glutamic acid, and lysine.

Conclusions:

  • The Os1-Cl complex demonstrates multitargeting binding ability towards BSA.
  • ECD MS/MS is an effective method for localizing metallocomplex binding sites on proteins.
  • This workflow provides a standard for analyzing metallocomplex interactions with biomolecules in complex biological systems.