清华大学刘凯研究小组报道，具有层次结构的动态多肽纳米诱导的蛋白自组装用于改善粘附性。这一研究成果于2025年1月9日发表在国际顶尖学术期刊《美国化学会杂志》上。

研究人员表示，等级结构在自然粘附系统中是必不可少的。由于复杂的分子机制和多尺度过程，在合成粘合剂中复制这些是具有挑战性的。

研究人员报道了三种磷酸化肽，它们具有与亲水性磷酸化序列（pSGSS）相连的疏水自组装基序，形成肽纤维纳米框架。这些纳米框架有效地与弹性蛋白衍生的带正电蛋白（PCP）共同组装，从而形成具有层次结构的复杂凝聚体基粘合剂。他们的方法能够控制粘合剂的内聚性和粘附性。

值得注意的是，由含二酪氨酸肽和PCP形成的复合粘合剂，具有高达30MPa的界面粘附强度，优于大多数已知的超分子粘合剂和交联化学粘合剂。此外，这些粘合剂显示出良好的生物相容性和生物活性，使其适用于内脏止血和组织修复等应用。

他们的发现强调了，生物启发的分层组装与生物工程技术相结合，在推进生物医学粘合剂方面的效用。

附：英文原文

Title: Dynamic Peptide Nanoframework-Guided Protein Coassembly: Advancing Adhesion Performance with Hierarchical Structures

Author: Yusai Zhou, Rong Chang, Zhenyue Yang, Qi Guo, Mengyao Wang, Bo Jia, Bo Li, Bodan Deng, Yubin Ren, Huaxia Zhu, Xinyan Wang, Qinrui Wang, Han Wen, Hongjie Zhang, Jing Yu, Yong-Xiang Chen, Kai Liu

Issue&Volume: January 9, 2025

Abstract: Hierarchical structures are essential in natural adhesion systems. Replicating these in synthetic adhesives is challenging due to intricate molecular mechanisms and multiscale processes. Here, we report three phosphorylated peptides featuring a hydrophobic self-assembly motif linked to a hydrophilic phosphorylated sequence (pSGSS), forming peptide fibril nanoframeworks. These nanoframeworks effectively coassemble with elastin-derived positively charged proteins (PCP), resulting in complex coacervate-based adhesives with hierarchical structures. Our method enables the controlled regulation of both cohesion and adhesion properties in the adhesives. Notably, the complex adhesives formed by the dityrosine-containing peptide and PCP demonstrate an exceptional interfacial adhesion strength of up to 30 MPa, outperforming most known supramolecular adhesives and rivaling cross-linked chemical adhesives. Additionally, these adhesives show promising biocompatibility and bioactivity, making them suitable for applications such as visceral hemostasis and tissue repair. Our findings highlight the utility of bioinspired hierarchical assembly combined with bioengineering techniques in advancing biomedical adhesives.

DOI: 10.1021/jacs.4c10882

Source: https://pubs.acs.org/doi/abs/10.1021/jacs.4c10882