Design and development of biocompatible nano- and mesosystems based on amyloid fibre formation

Operation co-funded by EU cohesion policy (European Regional Development Fund (ERDF)) under the programme Competitive Central-Hungary - ERDF/ESF (2014HU16M2OP002), managing authority: Nemzetgazdasági Minisztérium. Beneficiary: EÖTVÖS LORÁND TUDOMÁNYEGYETEM. Location: Budapest (NUTS HU110); Hungary. Budget: total eligible expenditure EUR 2,159,315.37; EU co-financing EUR 1,619,486.53 (co-financing rate 75%), as stated by the source. Runs 2017-09-01 to 2021-11-29. Source: Kohesio, EU cohesion policy projects managed by national and regional authorities (not CORDIS); selected because its summary names quantum technology. Summary from Kohesio (English machine translation by the source): Amyloid aggregation is of outstanding biomedical, bio- and structural-chemical importance and has attracted continued interest over the past decades (B.S. Blumberg and D.C. Gajdusek for Kuru’s disease (1976) and S.B. Prusiner for prion heritage understanding (1997) received the Nobel Medical Prize). Scientific breakthroughs in this area can only be achieved if there is a high degree of synergy between researchers, critical numbers and resources. The necessary synthetic, biochemical, spectroscopic, modelling, bioanalytical and nanotechnology capacity is now available at ELTE TTK. Our focus is the development of protein test systems, the rational design, in vitro/vivo production and development of biocompatible nanosystems. In order to achieve our research goals, we intend to establish a centre of excellence, which can bring significant breakthroughs in the field due to the development of cooperation across the whole field of molecular biochemistry, combining six different approaches and six different perspectives. Understanding the spatial structure and dynamics of proteins is a research task that is of biomedical, social and economic importance beyond chemical curiosity and importance. Proteins can be identified in almost all parts of living organisms and function effectively, in accordance with their environment, as complex systems, with well-regulated protein-protein interactions in the background, and with oligo and polymerisation processes (Tory, Perczel, Nature Genetics 2014). However, these processes sometimes lead to aggregation and amyloid dead ends. The change in conformation, which has been diagnosed by Alois Alzheimer for more than 100 years but has not yet been accurately understood on a molecular level, is only one of the amyloid aggregations experienced in the process of ‘protein ageing’. Aggregation is a thermodynamically beneficiary (Perczel 2007), and its detailed understanding and use are central elements of our application. In addition to [shortened; the full text is on the Kohesio page]

Original source.

Source: Kohesio (EU cohesion policy projects), European Commission, Directorate-General for Regional and Urban Policy (DG REGIO). Retrieved 2026-10-21. Licence: CC0 1.0 (Cohesion Open Data Platform, dataset 2014-2020 Kohesio projects). Selected metadata, adapted presentation; the publisher's record is authoritative. No endorsement by the source is implied. Licence: public domain dedication (CC0 1.0).

AI-assisted summary: The project focuses on the design and development of biocompatible nano- and mesosystems based on amyloid fibre formation, co-funded by the EU with a budget of EUR 2,159,315.37, running from September 2017 to November 2021 in Budapest, Hungary. Suggested technology pillar: enabling. Generated by AI from the public source text; it may contain errors and the original source is authoritative.