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Applied and Environmental Microbiology, March 2002, p. 1367-1373, Vol. 68, No. 3
0099-2240/02/$04.00+0 DOI: 10.1128/AEM.68.3.1367-1373.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
and Joseph G. H. Wessels1
Groningen Biotechnology and Biomolecular Sciences Institute, University of Groningen, 9751 NN Haren,1 Department of Biomedical Engineering, University of Groningen, 9713 AV Groningen,The Netherlands2
Received 4 September 2001/ Accepted 13 December 2001
Hydrophobins are small (ca. 100 amino acids) secreted fungal proteins that are characterized by the presence of eight conserved cysteine residues and by a typical hydropathy pattern. Class I hydrophobins self-assemble at hydrophilic-hydrophobic interfaces into highly insoluble amphipathic membranes, thereby changing the nature of surfaces. Hydrophobic surfaces become hydrophilic, while hydrophilic surfaces become hydrophobic. To see whether surface properties of assembled hydrophobins can be changed, 25 N-terminal residues of the mature SC3 hydrophobin were deleted (TrSC3). In addition, the cell-binding domain of fibronectin (RGD) was fused to the N terminus of mature SC3 (RGD-SC3) and TrSC3 (RGD-TrSC3). Self-assembly and surface activity were not affected by these modifications. However, physiochemical properties at the hydrophilic side of the assembled hydrophobin did change. This was demonstrated by a change in wettability and by enhanced growth of fibroblasts on Teflon-coated with RGD-SC3, TrSC3, or RGD-TrSC3 compared to bare Teflon or Teflon coated with SC3. Thus, engineered hydrophobins can be used to functionalize surfaces.
Present address: Microbiology, University of Utrecht, 3584 CH Utrecht, The Netherlands.
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