Date/Time Date(s) - 24/10/20241:30 pm - 2:20 pm
Title: Understanding the self-assembly mechanism of hydrophobin proteins to inform their design
Date: Thursday October 24, 2024
Time: 1:30-2:20pm
Room: ABB 165
Host: Dr. Giuseppe Melacini
Abstract: Hydrophobins are small, globular, and amphipathic proteins that are secreted by filamentous fungi. These proteins self-assemble at hydrophobic-hydrophilic interfaces into durable, water repellant, and amyloid-containing structures called rodlets. These unusual properties have given hydrophobins potential uses as tools to modify or functionalize surface properties, create water-repellent coatings, or as biological emulsifiers. Although hydrophobins have a conserved pattern of disulfide bonds and some atomic-resolution structures have been elucidated, the mechanism by which hydrophobins coat surfaces and self-assemble is currently unknown. My lab works to untangle the effects of protein structure and sequence composition on hydrophobin function by determining how hydrophobins self-assemble. We are pursuing this aim by characterizing the structure and function of diverse hydrophobins using nuclear magnetic resonance spectroscopy, X-ray crystallography, and atomic force microscopy. We integrate this data with functional assays to correlate hydrophobin sequence to function. Our results outline a fundamental mechanism of protein self-assembly and allow us to rationally design or functionalize hydrophobins with specific uses or properties mind.