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<p>Inflammation is a crucial immune response that protects the body from harmful stimuli; however, excessive or prolonged inflammation can lead to chronic inflammatory diseases. The IK protein, originally isolated from the K562 leukemia cell line, is known for its anti-inflammatory properties by downregulating inflammatory cytokine expression. A truncated form, tIK, exhibits similar regulatory effects. In this study, we designed short peptide derivatives of tIK, named tIK-9mer and -14mer, with potential anti-inflammatory activity. To elucidate their structural properties, we employed solution-state NMR spectroscopy to analyze the conformation of these peptides under different conditions, including the presence and absence of a membrane. Since the tIK protein is expected to exert its anti-inflammatory function by interacting with the IL-10 receptor (IL-10Rα), we investigated its membrane association as a preliminary step to understanding its mechanism. Additionally, given the structural and functional similarities between antimicrobial and anti-inflammatory peptides, we performed antimicrobial activity assays to assess whether tIK analogs possess antimicrobial properties. Our findings provide structural insights into tIK-derived peptides and lay the groundwork for their potential therapeutic applications in inflammatory diseases.</p>

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NMR backbone assignment of tIK peptides and their interactions with DPC micelles

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年11月18日

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  • Minseon Kim,
  • Jujin Park,
  • Yongae Kim

摘要

Inflammation is a crucial immune response that protects the body from harmful stimuli; however, excessive or prolonged inflammation can lead to chronic inflammatory diseases. The IK protein, originally isolated from the K562 leukemia cell line, is known for its anti-inflammatory properties by downregulating inflammatory cytokine expression. A truncated form, tIK, exhibits similar regulatory effects. In this study, we designed short peptide derivatives of tIK, named tIK-9mer and -14mer, with potential anti-inflammatory activity. To elucidate their structural properties, we employed solution-state NMR spectroscopy to analyze the conformation of these peptides under different conditions, including the presence and absence of a membrane. Since the tIK protein is expected to exert its anti-inflammatory function by interacting with the IL-10 receptor (IL-10Rα), we investigated its membrane association as a preliminary step to understanding its mechanism. Additionally, given the structural and functional similarities between antimicrobial and anti-inflammatory peptides, we performed antimicrobial activity assays to assess whether tIK analogs possess antimicrobial properties. Our findings provide structural insights into tIK-derived peptides and lay the groundwork for their potential therapeutic applications in inflammatory diseases.