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<p>Charged polymer interactions govern biological and technological processes by altering the structure and dynamics of surrounding water. Studying these interactions across a broad concentration range is challenging, particularly at submicromolar levels where traditional methods lack sensitivity or molecular resolution. Here, we investigate interactions between hyaluronan (HA), a biologically and technologically relevant polymer, and model oligopeptides—nonaarginine, nonalysine, and nonaglycine. By combining angle-resolved second harmonic scattering (AR-SHS), dynamic light scattering, nuclear magnetic resonance, and all-atom molecular dynamics simulations, we resolve the molecular-scale mechanisms and structure of HA–peptide interactions. Our findings reveal selective, multivalent binding between HA and cationic peptides, inducing solvent and solute restructuring and nanoscale clustering. Simulations provide atomic-level insight, elucidating the transient nature of the interactions and highlighting the distinctive behavior of arginine-rich peptides. Our approach, integrating AR-SHS with simulations and routine techniques, offers molecular insights into polymer mixtures and a foundation for future studies of dynamic supramolecular systems in soft materials.</p><p></p>

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Transient formation of supramolecular complexes between hyaluronan and oligopeptides at submicromolar concentration

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年1月13日

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  • Miguel Riopedre-Fernandez,
  • Bingxin Chu,
  • Anna Kuffel,
  • Arianna Marchioro,
  • Denys Biriukov,
  • Hector Martinez-Seara

摘要

Charged polymer interactions govern biological and technological processes by altering the structure and dynamics of surrounding water. Studying these interactions across a broad concentration range is challenging, particularly at submicromolar levels where traditional methods lack sensitivity or molecular resolution. Here, we investigate interactions between hyaluronan (HA), a biologically and technologically relevant polymer, and model oligopeptides—nonaarginine, nonalysine, and nonaglycine. By combining angle-resolved second harmonic scattering (AR-SHS), dynamic light scattering, nuclear magnetic resonance, and all-atom molecular dynamics simulations, we resolve the molecular-scale mechanisms and structure of HA–peptide interactions. Our findings reveal selective, multivalent binding between HA and cationic peptides, inducing solvent and solute restructuring and nanoscale clustering. Simulations provide atomic-level insight, elucidating the transient nature of the interactions and highlighting the distinctive behavior of arginine-rich peptides. Our approach, integrating AR-SHS with simulations and routine techniques, offers molecular insights into polymer mixtures and a foundation for future studies of dynamic supramolecular systems in soft materials.