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<p>Suppressing amyloid β (Aβ) aggregation is a promising therapeutic strategy for Alzheimer’s disease. We previously showed that the ovalbumin <i>N</i>-terminal peptide (pN) self-assembles and modestly inhibits Aβ<sub>42</sub> fibril formation. Here we prepared pN variants differing in net charge and examined how their self-assembled nanostructures affect Aβ<sub>42</sub> fibril formation. For each variant, we measured surface hydrophobicity and ζ-potential, and related them to fibril-formation kinetics. Across variants, inhibitory efficacy correlated with the coexistence of positive charge and surface hydrophobicity. Reducing hydrophobicity while retaining cationic character further strengthened inhibition, indicating that a balance between electrostatic and hydrophobic interactions governs inhibition.</p> Graphical abstract <p></p>

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Tuning charge and hydrophobicity in ovalbumin-derived peptide nanostructures enhances inhibition of Aβ42 fibril formation

  • 期刊论文

  • 发表日期：

    2026年2月13日

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  • Tomonori Waku,
  • Mei Wada,
  • Michiaki Okuda,
  • Hachiro Sugimoto,
  • Kazuya Matsuo,
  • Akio Kobori

摘要

Suppressing amyloid β (Aβ) aggregation is a promising therapeutic strategy for Alzheimer’s disease. We previously showed that the ovalbumin N-terminal peptide (pN) self-assembles and modestly inhibits Aβ42 fibril formation. Here we prepared pN variants differing in net charge and examined how their self-assembled nanostructures affect Aβ42 fibril formation. For each variant, we measured surface hydrophobicity and ζ-potential, and related them to fibril-formation kinetics. Across variants, inhibitory efficacy correlated with the coexistence of positive charge and surface hydrophobicity. Reducing hydrophobicity while retaining cationic character further strengthened inhibition, indicating that a balance between electrostatic and hydrophobic interactions governs inhibition.

Graphical abstract