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Polyphenol‐Mediated Assembly of Proteins for Engineering Functional Materials
Ist Teil von
Angewandte Chemie International Edition, 2020-09, Vol.59 (36), p.15618-15625
Auflage
International ed. in English
Ort / Verlag
Germany: Wiley Subscription Services, Inc
Erscheinungsjahr
2020
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
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).
In a material world: A simple and versatile strategy for assembling functional materials was established through the interfacial assembly of proteins and polyphenols on various substrates. Protein–polyphenol capsules were used to elucidate the dominant interaction(s) between different proteins and polyphenols. The assembled proteins retain their structure and function, thereby enabling their use in various applications, for example, biocatalysis or cell targeting.