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<p><i>Acinetobacter baumannii (A. baumannii</i>), a common hospital-associated pathogen, is known for its rapid ability to develop antibacterial drug resistance. The HIS-C enzyme in this pathogen is essential for histidine biosynthesis, making this a prominent drug target for antimicrobial therapy. This experimental investigation analyzes the inhibitory function of quercetin, a well-known antibacterial flavonoid, on HIS-C enzyme through the in vitro and in silico approaches. The binding affinity between quercetin and HIS-C was further examined through in vitro assays. Further, the surface plasmon resonance (SPR) experiments confirmed the strong binding affinity, with a dissociation constant (KD) of 3.3 × 10<sup>-6</sup> M. Antibacterial assays proved the inhibitory potential of quercetin against <i>A. baumannii</i> growth, with a minimum inhibitory concentration (MIC) of 15&#xa0;µg/mL. In silico analyses were performed to support these experimental results&#xa0;by&#xa0;providing additional insights into the binding interactions. Altogether, these in vitro and in silico findings have significantly proven the potential of quercetin as an HIS-C inhibitor. Further in vivo studies, particularly on toxicity and pharmacokinetics, are essential before it can be considered for therapeutic application against <i>A. baumannii</i> infections.</p>

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Quercetin as a promising HIS-C inhibitor and novel therapeutic against antibacterial drug-resistant Acinetobacter baumannii: in vitro and in silico insights

  • 期刊论文

  • 发表日期：

    2025年11月20日

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  • Mohammed Salleh M. Ardawi,
  • Samar A. Badreddine,
  • Muhammad Yasir,
  • Safaa A. Turkistani,
  • Ahmed Afandi,
  • Abdulaziz A. Kimawi,
  • Samah O. Noor,
  • Adhari Alselmi,
  • Salma Mohammed Alsayed,
  • Mada S. Alharthi,
  • Vivek Dhar Dwivedi,
  • Pradeep Sharma,
  • Esam I. Azhar

摘要

Acinetobacter baumannii (A. baumannii), a common hospital-associated pathogen, is known for its rapid ability to develop antibacterial drug resistance. The HIS-C enzyme in this pathogen is essential for histidine biosynthesis, making this a prominent drug target for antimicrobial therapy. This experimental investigation analyzes the inhibitory function of quercetin, a well-known antibacterial flavonoid, on HIS-C enzyme through the in vitro and in silico approaches. The binding affinity between quercetin and HIS-C was further examined through in vitro assays. Further, the surface plasmon resonance (SPR) experiments confirmed the strong binding affinity, with a dissociation constant (KD) of 3.3 × 10-6 M. Antibacterial assays proved the inhibitory potential of quercetin against A. baumannii growth, with a minimum inhibitory concentration (MIC) of 15 µg/mL. In silico analyses were performed to support these experimental results by providing additional insights into the binding interactions. Altogether, these in vitro and in silico findings have significantly proven the potential of quercetin as an HIS-C inhibitor. Further in vivo studies, particularly on toxicity and pharmacokinetics, are essential before it can be considered for therapeutic application against A. baumannii infections.