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Tuning the lanthanide binding tags for preferential actinide chelation: an all atom molecular dynamics study.

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Mutant peptides were designed to selectively bind trivalent actinide ions over lanthanide ions. Modifications to the lanthanide binding tag (LBT) peptide enhanced binding affinity and selectivity for actinides, aiding in separation processes.

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Area of Science:

  • Biochemistry and Molecular Biophysics
  • Radiochemistry and Nuclear Chemistry
  • Computational Chemistry and Molecular Modeling

Background:

  • The lanthanide binding tag (LBT) is a 17-amino acid peptide with high affinity for lanthanide (Ln3+) ions.
  • Selective separation of trivalent actinide (An3+) ions from lanthanides is crucial for nuclear waste management and remediation.
  • Existing LBT peptides show high affinity for Ln3+ but lack selectivity for An3+ over Ln3+.

Purpose of the Study:

  • To design mutant peptides derived from LBT with enhanced selectivity for An3+ over Ln3+ ions.
  • To investigate the binding dynamics and affinities of modified LBT peptides with representative An3+ (Am3+) and Ln3+ (Eu3+) ions.
  • To explore the potential of cysteine substitutions in modulating metal ion binding preferences.

Main Methods:

  • Design and synthesis of four LBT mutant peptides: M-LBT (wild-type), M-N103C, M-D105C, and M-N103C-D105C.
  • All-atom molecular dynamics (MD) simulations to analyze binding dynamics and affinities.
  • Enhanced sampling using well-tempered meta-dynamics (WT-MtD) to calculate converged free energy profiles for metal-binding interactions.

Main Results:

  • Mutations altered the peptide's binding pocket coordination environment, increasing selectivity for Am3+ over Eu3+.
  • The wild-type LBT showed an unbinding energy barrier of ~60 kJ mol-1 for Eu3+/Am3+.
  • The N103C mutant exhibited increased binding strength (>100 kJ mol-1), D105C showed Am3+ preference (~70 kJ mol-1), and N103C-D105C favored Am3+ by >20 kJ mol-1.

Conclusions:

  • The N103C mutant is suitable for general chelation of metal ions.
  • The N103C-D105C double mutant demonstrates significant preference for Am3+, enabling preferential trivalent actinide separation.
  • These engineered peptides offer promising applications as selective chelating agents for actinide binding and separation.