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Single‐Molecule Force Spectroscopy Reveals Self‐Assembly Enhanced Surface Binding of Hydrophobins
Author(s) -
Li Bing,
Wang Xin,
Li Ying,
Paananen Arja,
Szilvay Géza R.,
Qin Meng,
Wang Wei,
Cao Yi
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201801730
Subject(s) - hydrophobin , force spectroscopy , cooperativity , amphiphile , adhesion , molecule , nanoscopic scale , nanotechnology , materials science , adhesive , self assembly , chemistry , atomic force microscopy , copolymer , organic chemistry , biochemistry , composite material , polymer , layer (electronics) , gene
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.