RESUMEN
Biomolecular self-assembly of hierarchical materials is a precise and adaptable bottom-up approach to synthesizing across scales with considerable energy, health, environment, sustainability, and information technology applications. To achieve desired functions in biomaterials, it is essential to directly observe assembly dynamics and structural evolutions that reflect the underlying energy landscape and the assembly mechanism. This review will summarize the current understanding of biomolecular assembly mechanisms based on in situ characterization and discuss the broader significance and achievements of newly gained insights. In addition, we will also introduce how emerging deep learning/machine learning-based approaches, multiparametric characterization, and high-throughput methods can boost the development of biomolecular self-assembly. The objective of this review is to accelerate the development of in situ characterization approaches for biomolecular self-assembly and to inspire the next generation of biomimetic materials.
Asunto(s)
Materiales Biomiméticos , Materiales Biomiméticos/química , Materiales BiocompatiblesAsunto(s)
Grafito/química , Microscopía Electrónica de Transmisión , Proteínas/química , Bacillaceae/metabolismo , Proteínas Bacterianas/química , Proteínas Bacterianas/metabolismo , Congelación , Proteínas de Transporte de Monosacáridos/química , Proteínas de Transporte de Monosacáridos/metabolismo , Nanoestructuras/química , Proteínas/metabolismoRESUMEN
We have developed a multistep route to the fabrication of virus assembled nanostructures with chemoselective protein-to-surface linkers synthesized by an efficient solid-phase method. These linkers were used to create patterns of 30-to-50-nm-width-lines by scanning probe nanolithography. Genetically modified cow pea mosaic virus with unique cysteine residues at specific locations on their capsomers were assembled through covalent linkage on these patterns. The morphology of the assembled structures on these line patterns characterized by atomic force microscopy was found to be strongly influenced by the intervirion interactions.