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    Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein

    Year: 2017

    Journal: ACS Omega, Volume 2, OCT, page 6906–6915

    Authors: Griffo, Alessandra; Haehl, Hendrik; Grandthyll, Samuel; Mueller, Frank; Paananen, Arja; Ilmen, Marja; Szilvay, Geza R.; Landowski, Christopher P.; Penttila, Merja; Jacobs, Karin; Laaksonen, Paivi

    The adhesive and mechanical properties of a modular fusion protein consisting of two different types of binding units linked together via a flexible resilin-like-polypeptide domain are quantified. The adhesive domains have been constructed from fungal cellulose-binding modules (CBMs) and an amphiphilic hydrophobin HFBI. This study is carried out by single-molecule force spectroscopy, which enables stretching of single molecules. The fusion proteins are designed to self-assemble on the cellulose surface, leading into the submonolayer of proteins having the HFBI pointing away from the surface. A hydrophobic atomic force microscopy (AFM) tip can be employed for contacting and lifting the single fusion protein from the HFBI-functionalized terminus by the hydrophobic interaction between the tip surface and the hydrophobic patch of the HFBI. The work of rupture, contour length at rupture and the adhesion forces of the amphiphilic end domains are evaluated under aqueous environment at different pHs.
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