281394 Design, Synthesis and Characterization of Protein-Based Surfactants As Functional Drug Stabilizers
Over the past 2 decades, surfactants have grown into a
$20 billion annual business, with approximately 60% dedicated to industrial processes, 25% to
household products and 15% in specialty applications. Most noteworthy is the emergence of specialty
applications in the past 10 years, driven in large part by new areas such as biofuels, food
preservatives and design of biocompatible interfaces for diagnostics and delivery systems, which
require higher-cost, biodegradable materials whose phase behavior can be controlled through a
molecular ‘switch’ or tunable property. Our group has been investigating the hydrophobins, which are
a class of small (< 10 kDa), cysteine-rich peptides secreted by filamentous fungi in response to
pesticides, organic solvents or elevated temperatures, creating a water- and pesticide-repellant
surface. Despite their unique combination of biological (low immune response, biodegradable) and
chemical (low CAC, water-repellant) properties, relatively little is known in terms of the structural
features that give rise to their unique biological and chemical properties. I will describe our efforts to
develop high-yield methods for overproduction of hydrophobins, as well as a detailed biophysical
characterization of hydrophobin structure in solution to understand the molecular basis for their self-assembly.
Our more recent efforts to engineer novel, ‘switchable’ functions into designed variants of
hydrophobins will also be discussed
See more of this Group/Topical: Food, Pharmaceutical & Bioengineering Division - See also TI: Comprehensive Quality by Design in Pharmaceutical Development and Manufacture