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<p>6% hydroxyethyl starch (HES 130/0.4) is frequently employed to address hypovolemia, ensuring sufficient organ perfusion and oxygen transport. The effects on Apolipoprotein A-I (ApoA-I) were examined at three temperatures—280, 295, and 310&#xa0;K—through several spectroscopic techniques to explore its possible interaction with the predominant protein in veins. The experimental findings indicated that HES 130/0.4 efficiently extinguished the intrinsic fluorescence of APOA-I. We also assessed the binding sites, binding constant, and thermodynamic parameters, which indicated that HES 130/0.4 can spontaneously associate with APOA-I via hydrogen bonds and van der Waals interactions (Δ<i>G</i> =  − 1.93 × 10<sup>4</sup>&#xa0;J·mol<sup>−1</sup>, Δ<i>H</i> =  − 5.63 × 10<sup>4</sup>&#xa0;J&#xa0;mol⁻<sup>1</sup>, and Δ<i>S</i> =  − 119&#xa0;J&#xa0;mol⁻<sup>1</sup>&#xa0;K⁻<sup>1</sup>) with a single binding site and week binding forces (<i>n</i> = 1.03 and <i>K</i><sub><i>A</i></sub> = 1.78 × 10<sup>3</sup>&#xa0;M<sup>−1</sup>) at body temperature. Moreover, the structure of APOA-I was significantly altered in the presence of HES 130/0.4. Blood Ca<sup>2+</sup> and Fe<sup>3+</sup> will diminish the storage duration. The study provides accurate and thorough foundational data to clarify the binding mechanisms of HES 130/0.4 with APOA-I in vitro, which may help the comprehension of its impact on protein function and toxic mechanism during transit and distribution in the bloodstream.</p>

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Structural Changes of Apolipoprotein A-I Caused by Hydroxyethyl Starch 130/0.4 Reveals Potential Toxic Mechanisms

  • 期刊论文

  • 发表日期：

    2025年8月30日

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  • Lingyan Qu,
  • Liqun Jia,
  • Jianzhong Zhang,
  • Shuqin Ni

摘要

6% hydroxyethyl starch (HES 130/0.4) is frequently employed to address hypovolemia, ensuring sufficient organ perfusion and oxygen transport. The effects on Apolipoprotein A-I (ApoA-I) were examined at three temperatures—280, 295, and 310 K—through several spectroscopic techniques to explore its possible interaction with the predominant protein in veins. The experimental findings indicated that HES 130/0.4 efficiently extinguished the intrinsic fluorescence of APOA-I. We also assessed the binding sites, binding constant, and thermodynamic parameters, which indicated that HES 130/0.4 can spontaneously associate with APOA-I via hydrogen bonds and van der Waals interactions (ΔG =  − 1.93 × 104 J·mol−1, ΔH =  − 5.63 × 104 J mol⁻1, and ΔS =  − 119 J mol⁻1 K⁻1) with a single binding site and week binding forces (n = 1.03 and KA = 1.78 × 103 M−1) at body temperature. Moreover, the structure of APOA-I was significantly altered in the presence of HES 130/0.4. Blood Ca2+ and Fe3+ will diminish the storage duration. The study provides accurate and thorough foundational data to clarify the binding mechanisms of HES 130/0.4 with APOA-I in vitro, which may help the comprehension of its impact on protein function and toxic mechanism during transit and distribution in the bloodstream.