7xa4
Thermotoga maritima ferritin variant-Tm-E (S111H) with Zn
Structural highlights
FunctionQ9X0L2_THEMA Iron storage protein (By similarity).[RuleBase:RU361145] Publication Abstract from PubMedEngineering proteins to construct self-assemblies is of crucial significance not only for understanding the sophisticated living systems but also for fabricating advanced materials with unexplored functions. However, due to the inherent chemical heterogeneity and structural complexity of the protein surface, designing complex protein assemblies in an anisotropic fashion remains challenging. Here, we describe a self-assembly approach to fabricating protein origami with a networklike structure by designing dual noncovalent interactions on the different positions of a single protein building block. With dimeric proteins as building blocks, 1D protein filaments were constructed by the designed metal coordination at key protein interfaces. Subsequently, the network superstructures were created by the cross-linking of the 1D protein filaments at branch point linkages through the second designed pi-pi stacking interactions. Notably, upon increasing the protein concentration, the formed protein networks convert into hydrogels with reversible, injectable, and self-healing properties, which have the ability to promote bone regeneration. This strategy could be used to fabricate other protein-based materials with unexplored functions. Directed Self-Assembly of Dimeric Building Blocks into Networklike Protein Origami to Construct Hydrogels.,Liu Y, Chen X, Yin S, Chang X, Lv C, Zang J, Leng X, Zhang T, Zhao G ACS Nano. 2022 Nov 22;16(11):19472-19481. doi: 10.1021/acsnano.2c09391. Epub 2022 , Oct 31. PMID:36315654[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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