Scholarlink

<p>Amyloid-like proteins are critical for interfacial adhesion across various marine organisms and bacteria. However, the specific contributions of different functional residues remain unclear. Herein, we introduce an approach to deconstruct and mimic these residues using synthetic homopolymers and random copolymers with phenyl, amino, carboxyl, and hydroxyl functional groups using reversible addition-fragmentation chain transfer (RAFT) polymerization. The resulting polymers, designed with comparable molecular weights (<i>M</i><sub>n</sub>: 10–20 kDa) and narrow dispersities (PDI&lt;1.3), mimic the diverse surface chemistry of amyloid-like proteins, enabling systematic investigation of their adhesive properties. The interfacial adhesion forces of different polymer films were quantified using atomic force microscopy (AFM) with a colloidal probe. Remarkably, copolymers with multiple functional groups demonstrated significantly enhanced adhesion compared to homopolymers, a trend corroborated by macroscopic shear strength and stability tests. These results highlight that the synergistic effects of multiple functional groups are crucial for achieving universal interfacial adhesion of macromolecules, offering insights into protein adhesion mechanisms, and guiding polymer-based interfacial modifications.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Synergistic Functional Group Interactions for Stable Interfacial Adhesion: Insights from Amyloid-inspired Polymers

  • 期刊论文

  • 发表日期：

    2025年3月13日

查看全文
  • Jin-Wei Bai,
  • Wei Liu,
  • Bin Wen,
  • Zhong-Li Lei,
  • Chen Li,
  • Hao Ren,
  • Peng Yang

摘要

Amyloid-like proteins are critical for interfacial adhesion across various marine organisms and bacteria. However, the specific contributions of different functional residues remain unclear. Herein, we introduce an approach to deconstruct and mimic these residues using synthetic homopolymers and random copolymers with phenyl, amino, carboxyl, and hydroxyl functional groups using reversible addition-fragmentation chain transfer (RAFT) polymerization. The resulting polymers, designed with comparable molecular weights (Mn: 10–20 kDa) and narrow dispersities (PDI<1.3), mimic the diverse surface chemistry of amyloid-like proteins, enabling systematic investigation of their adhesive properties. The interfacial adhesion forces of different polymer films were quantified using atomic force microscopy (AFM) with a colloidal probe. Remarkably, copolymers with multiple functional groups demonstrated significantly enhanced adhesion compared to homopolymers, a trend corroborated by macroscopic shear strength and stability tests. These results highlight that the synergistic effects of multiple functional groups are crucial for achieving universal interfacial adhesion of macromolecules, offering insights into protein adhesion mechanisms, and guiding polymer-based interfacial modifications.