Single-Molecule Force Spectroscopy Reveals Self-Assembly Enhanced Surface Binding of Hydrophobins

Bing Li, Xin Wang, Ying Li, Arja Paananen, Géza R. Szilvay, Meng Qin, Wei Wang, Yi Cao

    Research output: Contribution to journalArticleScientificpeer-review

    12 Citations (Scopus)


    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 languageEnglish
    Pages (from-to)9224-9228
    JournalChemistry - A European Journal
    Issue number37
    Publication statusPublished - 2 Jul 2018
    MoE publication typeA1 Journal article-refereed


    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).


    • Force spectroscopy
    • Hydrophobin
    • Self-assembly
    • Single molecule
    • Surface adhesion


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