281394 Design, Synthesis and Characterization of Protein-Based Surfactants As Functional Drug Stabilizers

Wednesday, October 31, 2012
Hall B (Convention Center )
Rachael Barton1, Kevin Sledziewski2, Philo Morse2, Robert Lee2 and Bryan W. Berger3, (1)Chemical Engineering, Lehigh University, Bethlehem, PA, (2)Particle Sciences, Inc., Bethlehem, PA, (3)Chemical Engineering and Program in Bioengineering, Lehigh University, Bethlehem, PA

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

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