Explore the words cloud of the BETACONTROL project. It provides you a very rough idea of what is the project "BETACONTROL" about.
The following table provides information about the project.
|Coordinator Country||Germany [DE]|
|Total cost||1˙920˙697 €|
|EC max contribution||1˙920˙697 € (100%)|
1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
|Duration (year-month-day)||from 2017-06-01 to 2022-05-31|
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|1||HEINRICH-HEINE-UNIVERSITAET DUESSELDORF||DE (DUSSELDORF)||coordinator||1˙920˙697.00|
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|
Boran Uluca, Thibault Viennet, DuÅ¡an PetroviÄ‡, Hamed Shaykhalishahi, Franziska Weirich, AyÅŸenur GÃ¶nÃ¼lalan, Birgit Strodel, Manuel Etzkorn, Wolfgang Hoyer, Henrike Heise
DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of Î± -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|
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 Î²-wrapins
published pages: 322-332, ISSN: 0098-1354, DOI: 10.1016/j.compchemeng.2018.02.013
|Computers & Chemical Engineering 116||2019-06-12|
Thibault Viennet, Michael M. WÃ¶rdehoff, 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 Î±-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|
Filip Hasecke, Tatiana Miti, Carlos Perez, Jeremy Barton, Daniel SchÃ¶lzel, Lothar Gremer, Clara S. R. GrÃ¼ning, 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|
Michael M. WÃ¶rdehoff, Hamed Shaykhalishahi, Luca GroÃŸ, Lothar Gremer, Matthias Stoldt, Alexander K. Buell, Dieter Willbold, Wolfgang Hoyer
Opposed Effects of Dityrosine Formation in Soluble and Aggregated Î±-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|
Lothar Gremer, Daniel SchÃ¶lzel, Carla Schenk, Elke Reinartz, JÃ¶rg Labahn, Raimond B. G. Ravelli, Markus Tusche, Carmen Lopez-Iglesias, Wolfgang Hoyer, Henrike Heise, Dieter Willbold, Gunnar F. SchrÃ¶der
Fibril structure of amyloid-Î²(1â€“42) by cryoâ€“electron microscopy
published pages: 116-119, ISSN: 0036-8075, DOI: 10.1126/science.aao2825
Michael WÃ¶rdehoff, Wolfgang Hoyer
Î±-Synuclein Aggregation Monitored by Thioflavin T Fluorescence Assay
published pages: , ISSN: 2331-8325, DOI: 10.21769/BioProtoc.2941
Nadine S. RÃ¶sener, Lothar Gremer, Elke Reinartz, Anna KÃ¶nig, Oleksandr Brener, Henrike Heise, Wolfgang Hoyer, Philipp Neudecker, Dieter Willbold
A d-enantiomeric peptide interferes with heteroassociation of amyloid-Î² 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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