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 |
| Number of pages | 5 |
| Journal | Chemistry - A European Journal |
| Volume | 24 |
| Issue number | 37 |
| DOIs | |
| Publication status | Published - 2 Jul 2018 |
| MoE publication type | A1 Journal article-refereed |
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Keywords
- Force spectroscopy
- Hydrophobin
- Self-assembly
- Single molecule
- Surface adhesion
Cite this
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Single-Molecule Force Spectroscopy Reveals Self-Assembly Enhanced Surface Binding of Hydrophobins. / Li, Bing; Wang, Xin; Li, Ying; Paananen, Arja; Szilvay, Géza R.; Qin, Meng; Wang, Wei; Cao, Yi.
In: Chemistry - A European Journal, Vol. 24, No. 37, 02.07.2018, p. 9224-9228.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Single-Molecule Force Spectroscopy Reveals Self-Assembly Enhanced Surface Binding of Hydrophobins
AU - Li, Bing
AU - Wang, Xin
AU - Li, Ying
AU - Paananen, Arja
AU - Szilvay, Géza R.
AU - Qin, Meng
AU - Wang, Wei
AU - Cao, Yi
PY - 2018/7/2
Y1 - 2018/7/2
N2 - 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.
AB - 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.
KW - Force spectroscopy
KW - Hydrophobin
KW - Self-assembly
KW - Single molecule
KW - Surface adhesion
UR - http://www.scopus.com/inward/record.url?scp=85047725000&partnerID=8YFLogxK
U2 - 10.1002/chem.201801730
DO - 10.1002/chem.201801730
M3 - Article
AN - SCOPUS:85047725000
VL - 24
SP - 9224
EP - 9228
JO - Chemistry - A European Journal
JF - Chemistry - A European Journal
SN - 0947-6539
IS - 37
ER -