{'fraction_non_alphanumeric': 0.018063583815028903, 'fraction_numerical': 0.002890173410404624, 'mean_word_length': 5.822660098522167, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Kinetics and control of self-assembly of ABH1 hydrophobin from the edible white button mushroom.

Hydrophobins are small fungal proteins that self-assemble at hydrophobic/hydrophilic interfaces to form stable, amyloid membranes that are resistant to denaturation. Their remarkable surface activity has driven intense research for their potential utility in biomedical and cosmetic applications. In this research, the self-assembly characteristics of the Class I hydrophobin ABH1 from Agaricus bisporus , the edible white button mushroom, were evaluated as a function of solution and interface properties, in an attempt to gain greater mechanistic understanding. The kinetics of self-assembly were examined using dynamic quartz crystal microbalance techniques in combination with AFM, ellipsometry, contact angle goniometry, light scattering, and circular dichroism spectroscopy. It was found that the strength of interfacial tension between two phases drives the speed of ABH1 assembly and that the nature and location of the molecular ordering was influenced by temperature. ABH1 demonstrates different characteristics and self-assembly properties than those reported for other Class I hydrophobins, including causing an instantaneous decrease in surface tension in aqueous solution and undergoing a direct transition to β-sheet conformation on self-assembly at elevated temperature.