Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 24, Issue 37, Pages 9224-9228Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201801730
Keywords
force spectroscopy; hydrophobin; self-assembly; single molecule; surface adhesion
Categories
Funding
- NSFC [11674153, 21522402, 11334004]
- PAPD of Jiangsu Higher Education
- Fundamental Research Funds for the Central Universities [020414380070, 020414380058, 020414380050]
Ask authors/readers for more resources
Hydrophobins have raised lots of interest as powerful surface adhesives. However, it remains largely unexplored how their strong and versatile surface adhesion is linked to their unique amphiphilic structural features. Here, we develop an AFM-based single-molecule force spectroscopy assay to quantitatively measure the binding strength of hydrophobin to various types of surfaces both in isolation and in preformed protein films. We find that individual class II hydrophobins (HFBI) bind strongly to hydrophobic surfaces but weakly to hydrophilic ones. After self-assembly into protein films, they show much stronger binding strength to both surfaces due to the cooperativity of different interactions at nanoscale. Such self-assembly enhanced surface binding may serve as a general design principle for synthetic bioactive adhesives.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available