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May 26, 2026Frontiers in MicrobiologyOpen Access

Quantifying arsenic-binding affinities of ArsR proteins via biomimetic self-assembly

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Authors

LCLiang CuiXZXi ZhangXSXiaohui Sun

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Overview

Randomized trial quantifies arsenic-binding affinities in ArsR proteins, suggesting implications for environmental bioremediation.

Key Points

  • This study aims to quantitatively assess the arsenic-binding affinities of ArsR proteins using a novel self-assembly technique.
  • Developed a biomimetic self-assembly approach for protein interaction without purification after initial validation.
  • Immobilized ArsR on biosilica spheres to create a solid-phase arsenic adsorbent for binding affinity measurement.
  • Characterized nine ArsR homologs from Rhodopseudomonas palustris CGA009.
  • RpArsR1 and RpArsR2 displayed the highest binding affinity constants (K A > 10^7 M) for As(III).
  • Binding affinities were influenced by cysteine content and structural context.
  • RpArsR2 significantly reduced As(III) accumulation in plants, indicating potential for bioremediation.

Cite This Study

Cui et al. (2026) studied this question.

synapsesocial.com/papers/6a153801b5d9c58d83e8c306https://doi.org/10.3389/fmicb.2026.1846435
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