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Control of amyloid formation via beta-hairpin molecular recognition features

Total Cost €


EC-Contrib. €






Project "BETACONTROL" data sheet

The following table provides information about the project.


Organization address
postcode: 40225

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 Germany [DE]
 Total cost 1˙920˙697 €
 EC max contribution 1˙920˙697 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2016-COG
 Funding Scheme ERC-COG
 Starting year 2017
 Duration (year-month-day) from 2017-06-01   to  2022-05-31


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 


 Project objective

The aggregation of proteins into amyloid fibrils is involved in various diseases which place a high burden on patients, families, caregivers, and healthcare systems, including Alzheimer’s disease, Parkinson’s disease and type 2 diabetes. While the therapeutic potential of the inhibition of amyloid formation and spreading has been recognized, there is a lack of effective strategies targeting the early steps of the aggregation reaction.

In BETACONTROL, I want to establish a structure-guided approach to the control of amyloid formation and spreading. I will develop small molecule and polypeptide-based ligands that interfere with the initial phases of amyloid formation and thereby suppress any toxic oligomeric or fibrillar assemblies. The ligands will target beta-hairpin molecular recognition features, which I found to be readily accessible in disease-related amyloidogenic proteins. Targeting beta-hairpins enables retardation of protein aggregation by substoichiometric amounts of the ligand, affording inhibition of amyloid formation at low compound concentrations. As the strategy addresses the common propensity of amyloidogenic proteins to adopt beta-structure, it will be applicable to a wide range of proteins associated with various diseases.

BETACONTROL will yield molecular-level insight into the mechanistic basis of amyloid formation and spreading. Furthermore, it will elucidate the significance of beta-hairpins as molecular recognition features in intrinsically disordered proteins (IDPs) and highlight the applicability of these features as targets for interference with protein-protein interactions of IDPs. Ultimately, BETACONTROL will provide a novel therapeutic approach to a range of devastating diseases.


year authors and title journal last update
List of publications.
2018 Boran Uluca, Thibault Viennet, Dušan Petrović, Hamed Shaykhalishahi, Franziska Weirich, Ayşenur Gönülalan, Birgit Strodel, Manuel Etzkorn, Wolfgang Hoyer, Henrike Heise
DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of α -Synuclein in Different States
published pages: 1614-1623, ISSN: 0006-3495, DOI: 10.1016/j.bpj.2018.02.011
Biophysical Journal 114/7 2019-06-12
2018 Asuka A. Orr, Hamed Shaykhalishahi, Ewa A. Mirecka, Sai Vamshi R. Jonnalagadda, Wolfgang Hoyer, Phanourios Tamamis
Elucidating the multi-targeted anti-amyloid activity and enhanced islet amyloid polypeptide binding of β-wrapins
published pages: 322-332, ISSN: 0098-1354, DOI: 10.1016/j.compchemeng.2018.02.013
Computers & Chemical Engineering 116 2019-06-12
2018 Thibault Viennet, Michael M. Wördehoff, Boran Uluca, Chetan Poojari, Hamed Shaykhalishahi, Dieter Willbold, Birgit Strodel, Henrike Heise, Alexander K. Buell, Wolfgang Hoyer, Manuel Etzkorn
Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation
published pages: , ISSN: 2399-3642, DOI: 10.1038/s42003-018-0049-z
Communications Biology 1/1 2019-06-12
2018 Filip Hasecke, Tatiana Miti, Carlos Perez, Jeremy Barton, Daniel Schölzel, Lothar Gremer, Clara S. R. Grüning, Garrett Matthews, Georg Meisl, Tuomas P. J. Knowles, Dieter Willbold, Philipp Neudecker, Henrike Heise, Ghanim Ullah, Wolfgang Hoyer, Martin Muschol
Origin of metastable oligomers and their effects on amyloid fibril self-assembly
published pages: 5937-5948, ISSN: 2041-6520, DOI: 10.1039/c8sc01479e
Chemical Science 9/27 2019-06-12
2017 Michael M. Wördehoff, Hamed Shaykhalishahi, Luca Groß, Lothar Gremer, Matthias Stoldt, Alexander K. Buell, Dieter Willbold, Wolfgang Hoyer
Opposed Effects of Dityrosine Formation in Soluble and Aggregated α-Synuclein on Fibril Growth
published pages: 3018-3030, ISSN: 0022-2836, DOI: 10.1016/j.jmb.2017.09.005
Journal of Molecular Biology 429/20 2019-06-12
2017 Lothar Gremer, Daniel Schölzel, Carla Schenk, Elke Reinartz, Jörg Labahn, Raimond B. G. Ravelli, Markus Tusche, Carmen Lopez-Iglesias, Wolfgang Hoyer, Henrike Heise, Dieter Willbold, Gunnar F. Schröder
Fibril structure of amyloid-β(1–42) by cryo–electron microscopy
published pages: 116-119, ISSN: 0036-8075, DOI: 10.1126/science.aao2825
Science 358/6359 2019-06-12
2018 Michael Wördehoff, Wolfgang Hoyer
α-Synuclein Aggregation Monitored by Thioflavin T Fluorescence Assay
published pages: , ISSN: 2331-8325, DOI: 10.21769/BioProtoc.2941
BIO-PROTOCOL 8/14 2019-05-14
2018 Nadine S. Rösener, Lothar Gremer, Elke Reinartz, Anna König, Oleksandr Brener, Henrike Heise, Wolfgang Hoyer, Philipp Neudecker, Dieter Willbold
A d-enantiomeric peptide interferes with heteroassociation of amyloid-β oligomers and prion protein
published pages: 15748-15764, ISSN: 0021-9258, DOI: 10.1074/jbc.RA118.003116
Journal of Biological Chemistry 293/41 2019-05-14

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