TY - JOUR
T1 - Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein
AU - Griffo, Alessandra
AU - Hähl, Hendrik
AU - Grandthyll, Samuel
AU - Müller, Frank
AU - Paananen, Arja
AU - Ilmén, Marja
AU - Szilvay, Géza
AU - Landowski, Christopher P.
AU - Penttilä, Merja
AU - Jacobs, Karin
AU - Laaksonen, Päivi
N1 - Funding Information:
*E-mail: [email protected] (P.L.). ORCID Païvi 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:
© 2017 American Chemical Society.
Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.
PY - 2017/10/31
Y1 - 2017/10/31
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85032639037&partnerID=8YFLogxK
U2 - 10.1021/acsomega.7b01133
DO - 10.1021/acsomega.7b01133
M3 - Article
C2 - 31457277
SN - 2470-1343
VL - 2
SP - 6906
EP - 6915
JO - ACS Omega
JF - ACS Omega
IS - 10
ER -