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  11. Calprotectin's Protein Structure Shields Ni-n(his) Bonds From Competing Agents

Calprotectin's Protein Structure Shields Ni-N(His) Bonds from Competing Agents

Zhuojian Lu1, Jingyuan Nie1, Ziling Wang2

  • 1State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, 210023, China.

The Journal of Physical Chemistry Letters
|January 27, 2025

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View abstract on PubMed

Summary
This summary is machine-generated.

The protein environment stabilizes the nickel-nitrogen (Ni-N(His)) bond, crucial for protein purification. This bond shows greater mechanical and kinetic stability within proteins compared to synthetic systems.

Area of Science:

  • Biochemistry
  • Biophysics
  • Protein Engineering

Background:

  • The Ni-N(His) coordination bond is vital for recombinant protein purification using Ni-NTA systems.
  • Previous research focused on synthetic Ni-NTA-Histag systems, leaving the influence of protein structure on bond strength less understood.

Purpose of the Study:

  • To quantify the Ni-N(His) bond strength within a biologically relevant protein, calprotectin.
  • To investigate the impact of the protein environment on the mechanical and kinetic stability of the Ni-N(His) bond.

Main Methods:

  • Utilized atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS).
  • Quantified rupture force and analyzed kinetic off-rates of the Ni-N(His) bond in calprotectin.
  • Assessed bond stability against competing agents and acidic conditions.

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Main Results:

  • The Ni-N(His) bond within calprotectin exhibits a rupture force of approximately 56 pN.
  • A significantly lower off-rate was observed in the protein system compared to synthetic systems, indicating enhanced stability.
  • The bond demonstrated reduced susceptibility to displacement by imidazole and greater stability under acidic conditions.

Conclusions:

  • Protein structure plays a critical role in stabilizing the mechanical and kinetic properties of the Ni-N(His) bond.
  • Findings provide insights into metal-ligand interactions within proteins and implications for protein purification strategies.