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MMA SIGNED

Molecular Mechanical Adhesives

Total Cost €

0

EC-Contrib. €

0

Partnership

0

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 MMA project word cloud

Explore the words cloud of the MMA project. It provides you a very rough idea of what is the project "MMA" about.

designing    rationally    extracellular    stable    breaking    broken    reversible    native    clotting    bond    components    adapt    mechanically    liquid    polymers    designed    frontier    dissipation    ground    leveraging    times    principles    gels    molecule    receptor    adhere    networks    pioneered    mimic    tunable    cohesins    made    doc    strength    handles    settings    adhesives    experiments    hydrogels    relied    oligomerized    combination    mixture    behavior    hydrogel    cells    biocompatible    protein    ligand    family    molecular    bulk    gel    super    mechanical    surgical    interpenetrating    engineering    domains    materials    coh    complexes    spray    possess    macroscale    bridging    energy    healing    consisting    mechanics    seamlessly    collagen    improvements    merge    mechano    tissues    poor    discoveries    self    attempts    modest    hampered    lies    macroscopic    influence    reformed    fibrin    nanomechanics    ligands    thousands    single    am    hypothesis    spontaneously    proteins    modes    covalent    stability    peo    dockerin    gap    form    matrix    sealants   

Project "MMA" data sheet

The following table provides information about the project.

Coordinator
UNIVERSITAT BASEL 

Organization address
address: PETERSPLATZ 1
city: BASEL
postcode: 4051
website: www.unibas.ch

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Switzerland [CH]
 Total cost 1˙466˙916 €
 EC max contribution 1˙466˙916 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2016-STG
 Funding Scheme ERC-STG
 Starting year 2017
 Duration (year-month-day) from 2017-04-01   to  2022-03-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    UNIVERSITAT BASEL CH (BASEL) coordinator 1˙466˙916.00

Map

 Project objective

Protein-based hydrogels are commonly used as adhesives and sealants in surgical settings. Fibrin gels, for example, are biocompatible, however their use is hampered by poor mechanical properties. Previous attempts to improve fibrin gel mechanics relied on interpenetrating networks in combination with PEO, collagen and other polymers, however, only modest improvements were observed. The important challenge lies in understanding how molecular design principles can influence gel mechanics on the macroscale.

The goal of this research is to develop mechanically tunable protein hydrogels. Upon mixture of two liquid components, the systems I propose would spontaneously form a gel matrix consisting of oligomerized proteins that mimic the extracellular matrix and possess controllable mechanical responses. By understanding protein nanomechanics at the single-molecule level, and designing modes of energy dissipation into hydrogel networks, my project will have an impact by bridging the knowledge gap between single-molecule and macroscopic mechanical responses.

My approach is ground-breaking because I am leveraging the discoveries I made on a family of super-stable receptor-ligand proteins (Cohesins & Dockerin (Coh-Doc)). These reversible receptor-ligands can be broken and reformed thousands of times, yet still maintain high stability (1/2 covalent bond strength). After having pioneered the application of these mechano-stable domains as molecular handles in single-molecule experiments, I propose the following frontier research:

A) I will use molecular engineering of Coh-Doc complexes to test the hypothesis that mechanical properties of bulk materials can be rationally designed based on single-molecule mechanical behavior of receptor-ligands. B) I will adapt the system to seamlessly merge with the native fibrin clotting pathway, providing a self-healing mechano-stable fibrin-based gel that could be applied as a liquid or spray and strongly adhere to cells and tissues.

 Publications

year authors and title journal last update
List of publications.
2019 Rafael C. Bernardi, Ellis Durner, Constantin Schoeler, Klara H. Malinowska, Bruna G. Carvalho, Edward A. Bayer, Zaida Luthey-Schulten, Hermann E. Gaub, Michael A. Nash
Mechanisms of Nanonewton Mechanostability in a Protein Complex Revealed by Molecular Dynamics Simulations and Single-Molecule Force Spectroscopy
published pages: 14752-14763, ISSN: 0002-7863, DOI: 10.1021/jacs.9b06776
Journal of the American Chemical Society 141/37 2019-12-16
2019 Haipei Liu, Valentin Schittny, Michael A. Nash
Removal of a Conserved Disulfide Bond Does Not Compromise Mechanical Stability of a VHH Antibody Complex
published pages: 5524-5529, ISSN: 1530-6984, DOI: 10.1021/acs.nanolett.9b02062
Nano Letters 19/8 2019-12-16
2018 Duy Tien Ta, Rosario Vanella, Michael A. Nash
Bioorthogonal Elastin-like Polypeptide Scaffolds for Immunoassay Enhancement
published pages: 30147-30154, ISSN: 1944-8244, DOI: 10.1021/acsami.8b10092
ACS Applied Materials & Interfaces 10/36 2019-05-27
2017 Wolfgang Ott, Markus A. Jobst, Magnus S. Bauer, Ellis Durner, Lukas F. Milles, Michael A. Nash, Hermann E. Gaub
Elastin-like Polypeptide Linkers for Single-Molecule Force Spectroscopy
published pages: 6346-6354, ISSN: 1936-0851, DOI: 10.1021/acsnano.7b02694
ACS Nano 11/6 2019-05-27
2017 Tobias Verdorfer, Rafael C. Bernardi, Aylin Meinhold, Wolfgang Ott, Zaida Luthey-Schulten, Michael A. Nash, Hermann E. Gaub
Combining in Vitro and in Silico Single-Molecule Force Spectroscopy to Characterize and Tune Cellulosomal Scaffoldin Mechanics
published pages: 17841-17852, ISSN: 0002-7863, DOI: 10.1021/jacs.7b07574
Journal of the American Chemical Society 139/49 2019-05-27
2018 Haipei Liu, Duy Tien Ta, Michael A. Nash
Mechanical Polyprotein Assembly Using Sfp and Sortase-Mediated Domain Oligomerization for Single-Molecule Studies
published pages: 1800039, ISSN: 2366-9608, DOI: 10.1002/smtd.201800039
Small Methods 2/6 2019-05-10

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