Self-assembly and aggregation behavior of the hydrophobins hypA and hypB from Agaricus bisporus

POLY 32

Lacey M. Harris, lacey.m.harris@gmail.com1, Jun Li1, Gordon C. Cannon, gordon.cannon@usm.edu2, Sabine Heinhorst2, and Sarah E. Morgan, sarah.morgan@usm.edu1. (1) School of Polymers and High Performance Materials, The University of Southern Mississippi, 118 College Dr., #10076, Hattiesburg, MS 39406, (2) Department of Chemistry and Biochemistry, The University of Southern Mississippi, S.S. Box 5043, Hattiesburg, MS 39406
Hydrophobins are naturally secreted fungal proteins with amphipathic characteristics. Due to unique structural properties, hydrophobins exhibit remarkable self-assembly and adhesive properties on surfaces and at interfaces. Two hydrophobins, hypA (ABH1) and hypB (ABH2), were isolated from the fruiting body of the basidiomycete Agaricus bisporus, commonly known as the white button mushroom. Samples of the hydrophobins isolated from both the entire body and peel tissue of the mushroom were evaluated in solution utilizing dynamic light scattering (DLS). Results show the proteins exist as multimers in solution, with aggregation dependent upon both salt concentration and pH. Film formation of the hydrophobins isolated from the entire body was also evaluated using atomic force microscopy (AFM). AFM indicated films exhibited features of similar dimensions to those observed in DLS.
 

Undergraduate Research in Polymer Science
8:15 AM-12:00 PM, Sunday, April 6, 2008 Hilton New Orleans Riverside -- Grand Salon 16, Oral

Division of Polymer Chemistry

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008