Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 9224-9228 |
| Journal | Chemistry - A European Journal |
| Volume | 24 |
| Issue number | 37 |
| DOIs | |
| Publication status | Published - 2 Jul 2018 |
| MoE publication type | A1 Journal article-refereed |
Funding
Y.C. and W.W. were financially supported by NSFC grants (11674153, 21522402, and 11334004), the PAPD of Jiangsu Higher Education, and the Fundamental Research Funds for the Central Universities (020414380070, 020414380058, and 020414380050). Work by A.P. and G.R.S. was carried out under Academy of Finland’s Centres of Excellence Programme (2014–2019).
Keywords
- Force spectroscopy
- Hydrophobin
- Self-assembly
- Single molecule
- Surface adhesion