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基于 Sn 触发的具有新兴功能的二维快速蛋白质组装。

Sn-Triggered Two-Dimensional Fast Protein Assembly with Emergent Functions.

机构信息

Key Laboratory of Applied Surface and Colloid Chemistry, Ministry of Education, School of Chemistry and Chemical Engineering , Shaanxi Normal University , Xi'an 710062 , P.R. China.

School and Hospital of Stomatology , Tianjin Medical University , 12 Observatory Road , Tianjin 30070 , P.R. China.

出版信息

ACS Nano. 2019 Jul 23;13(7):7736-7749. doi: 10.1021/acsnano.9b01392. Epub 2019 Jun 20.

DOI:10.1021/acsnano.9b01392
PMID:31244042
Abstract

The discovery of a general strategy for organizing functional proteins into stable nanostructures with the desired dimension, shape, and function is an important focus in developing protein-based self-assembled materials, but the scalable synthesis of such materials and transfer to other substrates remain great challenges. We herein tackle this issue by creating a two-dimensional metal-protein hybrid nanofilm that is flexible and cost-effective with reliable self-recovery, stability, and multifunctionality. As it differs from traditional metal ions, we discover the capability of Sn to initiate fast amyloid-like protein assembly (occurring in seconds) by effectively reducing the disulfide bonds of native globular proteins. The Sn-initiated lysozyme aggregation at the air/water interface leads to droplet flattening, a result never before reported in a protein system, which finally affords a multifunctional 2D Sn-doped hybrid lysozyme nanofilm with an ultralarge area (., 0.2 m) within a few minutes. The hybrid film is distinctive in its ease of coating on versatile material surfaces with endurable chemical and mechanical stability, optical transparency, and diverse end uses in antimicrobial and photo-/electrocatalytic scaffolds. Our approach provides not only insights into the effect of tin ions on macroscopic self-assembly of proteins but also a controllable and scalable synthesis of a potential biomimic framework for biomedical and biocatalytic applications.

摘要

将功能性蛋白质组织成具有所需维度、形状和功能的稳定纳米结构的通用策略的发现,是开发基于蛋白质的自组装材料的重要焦点,但此类材料的可扩展合成以及向其他基底的转移仍然是巨大的挑战。我们通过创建一种二维金属-蛋白质杂化纳米薄膜来解决这个问题,这种薄膜具有柔韧性、成本效益、可靠的自恢复性、稳定性和多功能性。与传统金属离子不同,我们发现 Sn 能够通过有效还原天然球状蛋白质的二硫键,快速引发类淀粉样蛋白组装(在几秒钟内发生)。Sn 引发的溶菌酶在气/水界面上的聚集导致液滴变平,这是蛋白质体系中从未报道过的结果,最终在几分钟内提供了具有超大面积(例如,0.2 m)的多功能二维 Sn 掺杂杂化溶菌酶纳米薄膜。该杂化薄膜的独特之处在于其易于在各种材料表面进行涂层,具有持久的化学和机械稳定性、光学透明度以及在抗菌和光/电催化支架等方面的多种用途。我们的方法不仅提供了关于锡离子对蛋白质宏观自组装影响的见解,而且还提供了一种用于生物医学和生物催化应用的潜在仿生框架的可控和可扩展的合成方法。

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引用本文的文献

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Synthesis and functionalization of scalable and versatile 2D protein films via amyloid-like aggregation.通过类淀粉样聚集合成可扩展且通用的二维蛋白质薄膜并进行功能化修饰。
Nat Protoc. 2024 Feb;19(2):539-564. doi: 10.1038/s41596-023-00918-4. Epub 2023 Dec 4.
2
Zwitterionic polymers-armored amyloid-like protein surface combats thrombosis and biofouling.两性离子聚合物包裹的类淀粉样蛋白表面可对抗血栓形成和生物污垢。
Bioact Mater. 2023 Sep 27;32:37-51. doi: 10.1016/j.bioactmat.2023.09.003. eCollection 2024 Feb.
3
Redox responsive activity regulation in exceptionally stable supramolecular assembly and co-assembly of a protein.
蛋白质在极其稳定的超分子组装和共组装中的氧化还原响应活性调控。
Chem Sci. 2020 Nov 17;12(3):1101-1108. doi: 10.1039/d0sc05312k.