Probing nanomechanical interactions of SARS-CoV-2 variants Omicron and XBB with common surfaces.

The emergence of SARS-CoV-2 variants has further raised concerns about viral transmission. A fundamental understanding of the intermolecular interactions between the coronavirus and different surfaces is needed to address the transmission of SARS-CoV-2 through respiratory droplet-contaminated surfaces or fomites. The receptor-binding domain (RBD) of the spike protein is a key target for the adhesion of SARS-CoV-2 on the surface.

S373P Mutation Stabilizes the Receptor-Binding Domain of the Spike Protein in Omicron and Promotes Binding.

A cluster of several newly occurring mutations on Omicron is found at the β-core region of the spike protein's receptor-binding domain (RBD), where mutation rarely happened before. Notably, the binding of SARS-CoV-2 to human receptor ACE2 via RBD happens in a dynamic airway environment, where mechanical force caused by coughing or sneezing occurs. Thus, we used atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to measure the stability of RBDs and found that the mechanical stability of Omicron RBD increased by ∼20% compared with the wild type.

Recombination and Purification of Elastin-Like Polypeptides.

Elastin, as an extracellular matrix protein, has inherent advantages for biomedical applications. For example, it is highly extensible and biocompatible, biodegradable, and has no immunogenicity. However, directly extracting elastin from biological tissues remains challenging because they usually coexist with other proteins such as collagen.

Synthesis and Assembly of Recombinant Collagen.

Collagen represents the major structural protein of the extracellular matrix. The desired mechanical and biological performances of collagen that have led to its broad applications as a building block in a great deal of fields, such as tissue engineering, drug delivery, and nanodevices. The most direct way to obtain collagen is to separate and extract it from biological tissues, but these top-down methods are usually cumbersome, and the structure of collagen is usually destroyed during the preparation process.

Structure of Resilin.

Resilin, an insect structural protein, exhibits rubberlike elasticity characterized by low stiffness, high extensibility, efficient energy storage, exceptional resilience, and fatigue lifetime. The outstanding mechanical properties of native resilin have motivated recent research about resilin-like biomaterials for a wide range of applications. The systematic understanding of the resilin structure provides theoretical guidance for its applications.

Structure of Elastin.

As the extracellular matrix protein, elastin is a crucial component of connective tissue in life. It is responsible for the structural integrity and function of tissues undergoing reversible extensibility or deformability, even though it may make up only a small percentage of a tissue. The structure stability, elastic resilience, bioactivity, and ability of self-assembly make elastin a highly desirable candidate for the fabrication of biomaterials.

Structure of Collagen.

Collagen is the most abundant fibrous protein in nature and widely exists in tissues such as connective tissue, tendon, skin, bone, and cartilage. On the one hand, collagen provides mechanical support in tissues, and on the other hand, plays an important role in controlling cell adhesion, cell migration, and tissue repair. A systematic understanding of the structure of collagen can promote the understanding of the biological functions of collagen scaffolds, and also provide theoretical guidance for applications of these natural fibrous protein materials.

Formation, Structure, and Mechanical Performance of Silk Nanofibrils Produced by Heat-Induced Self-Assembly.

The heat-induced self-assembly of silk fibroin (SF) is studied by combing fluorescence assessment, infrared nanospectroscopy, wide-angle X-ray scattering, and Derjaguin-Muller-Toporov coupled with atomic force microscopy. Several fundamental issues regarding the formation, structure, and mechanical performance of silk nanofibrils (SNFs) under heat-induced self-assembly are discussed. Accordingly, SF in aqueous solution is rod-like in shape and not micellar.