多酚
单宁酸
化学
变性(裂变材料)
功能(生物学)
纳米材料
非共价相互作用
氢键
生物物理学
纳米技术
蛋白质工程
生物化学
有机化学
材料科学
分子
生物
细胞生物学
酶
抗氧化剂
核化学
作者
Yiyuan Han,Zhixing Lin,Jiajing Zhou,Gyeongwon Yun,Rui Guo,Joseph J. Richardson,Frank Caruso
标识
DOI:10.1002/anie.202002089
摘要
Abstract Functional materials composed of proteins have attracted much interest owing to the inherent and diverse functionality of proteins. However, establishing general techniques for assembling proteins into nanomaterials is challenging owing to the complex physicochemical nature and potential denaturation of proteins. Here, a simple, versatile strategy is introduced to fabricate functional protein assemblies through the interfacial assembly of proteins and polyphenols (e.g., tannic acid) on various substrates (organic, inorganic, and biological). The dominant interactions (hydrogen‐bonding, hydrophobic, and ionic) between the proteins and tannic acid were elucidated; most proteins undergo multiple noncovalent stabilizing interactions with polyphenols, which can be used to engineer responsiveness into the assemblies. The proteins retain their structure and function within the assemblies, thereby enabling their use in various applications (e.g., catalysis, fluorescence imaging, and cell targeting).
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