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<p>In this study, the polymerization property of dopamine under alkaline conditions was exploited to tune the neutral (ζ ~ 2&#xa0;mV) and micron-sized zein–laponite coacervate. At [NaOH] &lt; 10&#xa0;mM, large (micron-sized) and unstable (ζ ≥ 18&#xa0;mV) dopamine-modified zein–laponite (DA–ZL) complexes undergoing dynamic self-assembly were formed, whereas at [NaOH] ≥ 10&#xa0;mM, smaller (D<sub>H</sub> &lt; 400&#xa0;nm) and stable (ζ ≤ 35&#xa0;mV) DA–ZL complexes undergoing static self-assembly were formed. The smaller and stable DA–ZL complexes were then used to evaluate their antioxidant and antibacterial activity when bound with gentamicin (GS). GS-bound DA–ZL complexes (MIC<sub>50</sub> = 5.6&#xa0;μM) showed higher antibacterial activity against <i>E. coli</i> than GS alone (MIC<sub>50</sub> = 15.4&#xa0;μM). The study suggested that ROS generation could be the probable antibacterial mechanism of the GS-bound DA–ZL&#xa0;complexes.</p> Graphical abstract <p></p>

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Dopamine-modified zein–laponite complexes for gentamicin delivery: A study on transition from dynamic to static self-assembly and efficacy against E. coli

  • 期刊论文

  • 发表日期：

    2025年11月14日

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  • Sara Dua,
  • Sonam Gupta,
  • Shama Parveen,
  • Najmul Arfin

摘要

In this study, the polymerization property of dopamine under alkaline conditions was exploited to tune the neutral (ζ ~ 2 mV) and micron-sized zein–laponite coacervate. At [NaOH] < 10 mM, large (micron-sized) and unstable (ζ ≥ 18 mV) dopamine-modified zein–laponite (DA–ZL) complexes undergoing dynamic self-assembly were formed, whereas at [NaOH] ≥ 10 mM, smaller (DH < 400 nm) and stable (ζ ≤ 35 mV) DA–ZL complexes undergoing static self-assembly were formed. The smaller and stable DA–ZL complexes were then used to evaluate their antioxidant and antibacterial activity when bound with gentamicin (GS). GS-bound DA–ZL complexes (MIC50 = 5.6 μM) showed higher antibacterial activity against E. coli than GS alone (MIC50 = 15.4 μM). The study suggested that ROS generation could be the probable antibacterial mechanism of the GS-bound DA–ZL complexes.

Graphical abstract