@article{b1cba020b1f847d782ef9ec23dc6462b,
title = "Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein",
abstract = "The adhesive and mechanical properties of a modular fusion protein consisting of two different types of binding units linked together via a flexible resilin-likepolypeptide 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.",
author = "Alessandra Griffo and Hendrik H{\"a}hl and Samuel Grandthyll and Frank M{\"u}ller and Arja Paananen and Marja Ilm{\'e}n and G{\'e}za Szilvay and Landowski, {Christopher P.} and Merja Penttil{\"a} and Karin Jacobs and P{\"a}ivi Laaksonen",
note = "Funding Information: *E-mail: paivi.laaksonen@aalto.fi (P.L.). ORCID Pa{\"i}vi Laaksonen: 0000-0003-2029-5275 Author Contributions The manuscript was written through contributions of all authors. All authors have given approval to the final version of the manuscript. Funding Funding for A.G. and P.L. has been granted from the Academy of Finland Center of Excellence Program via the “Center of Excellence in Molecular Engineering of Biosynthetic Hybrid Materials” (“HYBER”) and for A.G., H.H., S.G., F.M., and K.J. from the German Research Foundation (DFG) via the Collaborative Research Center SFB 1027 “Physical modeling of nonequilibrium processes in biological Systems”. Notes The authors declare no competing financial interest. Publisher Copyright: {\textcopyright} 2017 American Chemical Society. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.",
year = "2017",
month = oct,
day = "31",
doi = "10.1021/acsomega.7b01133",
language = "English",
volume = "2",
pages = "6906--6915",
journal = "ACS Omega",
issn = "2470-1343",
publisher = "American Chemical Society ACS",
number = "10",
}