Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein

Alessandra Griffo, Hendrik Hähl, Samuel Grandthyll, Frank Müller, Arja Paananen, Marja Ilmén, Géza Szilvay, Christopher P. Landowski, Merja Penttilä, Karin Jacobs, Päivi Laaksonen

Research output: Contribution to journalArticleScientificpeer-review

3 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)6906-6915
Number of pages10
JournalACS Omega
Volume2
Issue number10
DOIs
Publication statusPublished - 1 Jan 2017
MoE publication typeA1 Journal article-refereed

Fingerprint

Fusion reactions
Spectroscopy
Proteins
Molecules
Cellulose
Adhesives
Stretching
Atomic force microscopy
Adhesion
Mechanical properties
1-(heptafluorobutyryl)imidazole
resilin

Cite this

Griffo, A., Hähl, H., Grandthyll, S., Müller, F., Paananen, A., Ilmén, M., ... Laaksonen, P. (2017). Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein. ACS Omega, 2(10), 6906-6915. https://doi.org/10.1021/acsomega.7b01133
Griffo, Alessandra ; Hähl, Hendrik ; Grandthyll, Samuel ; Müller, Frank ; Paananen, Arja ; Ilmén, Marja ; Szilvay, Géza ; Landowski, Christopher P. ; Penttilä, Merja ; Jacobs, Karin ; Laaksonen, Päivi. / Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein. In: ACS Omega. 2017 ; Vol. 2, No. 10. pp. 6906-6915.
@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",
year = "2017",
month = "1",
day = "1",
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",

}

Single-Molecule Force Spectroscopy Study on Modular Resilin Fusion Protein. / Griffo, Alessandra; Hähl, Hendrik; Grandthyll, Samuel; Müller, Frank; Paananen, Arja; Ilmén, Marja; Szilvay, Géza; Landowski, Christopher P.; Penttilä, Merja; Jacobs, Karin; Laaksonen, Päivi.

In: ACS Omega, Vol. 2, No. 10, 01.01.2017, p. 6906-6915.

Research output: Contribution to journalArticleScientificpeer-review

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

PY - 2017/1/1

Y1 - 2017/1/1

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

VL - 2

SP - 6906

EP - 6915

JO - ACS Omega

JF - ACS Omega

SN - 2470-1343

IS - 10

ER -