The complex structure of represents an architectural design for high-performance ultralightweight materials.

High strength, hardness, and fracture toughness are mechanical properties that are not commonly associated with the fleshy body of a fungus. Here, we show with detailed structural, chemical, and mechanical characterization that is an exception, and its architectural design is a source of inspiration for an emerging class of ultralightweight high-performance materials. Our findings reveal that .

Quantifying biomolecular hydrophobicity: Single molecule force spectroscopy of class II hydrophobins.

Hydrophobins are surface-active proteins produced by filamentous fungi. The amphiphilic structure of hydrophobins is very compact, containing a distinct hydrophobic patch on one side of the molecule, locked by four intramolecular disulfide bridges. Hydrophobins form dimers and multimers in solution to shield these hydrophobic patches from water exposure.

Cellular agriculture - industrial biotechnology for food and materials.

Fundamental changes of agriculture and food production are inevitable. Providing food for an increasing population will be a great challenge that coincides with the pressure to reduce negative environmental impacts of conventional agriculture. Biotechnological manufacturing of acellular products for food and materials has already been piloted but the full profit of cellular agriculture is just beginning to emerge.

Single-Molecule Force Spectroscopy Reveals Self-Assembly Enhanced Surface Binding of Hydrophobins.

Hydrophobins have raised lots of interest as powerful surface adhesives. However, it remains largely unexplored how their strong and versatile surface adhesion is linked to their unique amphiphilic structural features. Here, we develop an AFM-based single-molecule force spectroscopy assay to quantitatively measure the binding strength of hydrophobin to various types of surfaces both in isolation and in preformed protein films.

Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein.

The adhesive and mechanical properties of a modular fusion protein consisting of two different types of binding units linked together via a flexible resilin-like-polypeptide domain are quantified. The adhesive domains have been constructed from fungal cellulose-binding modules (CBMs) and an amphiphilic hydrophobin HFBI. This study is carried out by single-molecule force spectroscopy, which enables stretching of single molecules.