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Trivalent actinides and lanthanides bind strongly to calmodulin (CaM), potentially disrupting cell signaling and causing organ accumulation. This study reveals their binding mechanisms and impact on CaM function.

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Area of Science:

  • Biochemistry
  • Computational Chemistry
  • Spectroscopy

Background:

  • Trivalent actinides and lanthanides pose health risks due to industrial activities like mining.
  • These ions exhibit high affinity for calmodulin (CaM), a crucial protein in cellular signaling.
  • Inadvertent uptake can lead to protein dysfunction and ion accumulation in human organs.

Purpose of the Study:

  • Investigate the effects of An3+ and Ln3+ ion substitution on CaM structure, enzymatic activity, and cytotoxicity.
  • Characterize the binding interactions between CaM and Cm3+/Eu3+ ions.
  • Understand the molecular mechanisms underlying CaM's response to these toxic metal ions.

Main Methods:

  • Spectroscopy
  • Computational chemistry (MP2 level, fragment molecular orbital method)
  • Calorimetry
  • Biochemistry

Main Results:

  • Cm3+ and Eu3+ show higher affinity for CaM than Ca2+ across all four binding sites.
  • A unique high-affinity site (EF-hand 3) exhibits exothermic binding for Eu3+, while other sites show endothermic binding due to hydration shell loss.
  • Binding of Cm3+/Eu3+ causes minor structural disorder in CaM and a slight decrease in enzymatic activity compared to Ca2+-CaM.

Conclusions:

  • Cm3+ and Eu3+ bind to CaM with high affinity, with distinct thermodynamic and structural consequences.
  • EF-hand 3's unique properties facilitate preferential binding of these trivalent ions.
  • The findings provide molecular insights into CaM-actinide/lanthanide interactions, relevant for understanding toxicity and developing mitigation strategies.