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GLAM-Map

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Global Amyloid Mapping Solving Amyloid Nucleation by Deep Mutagenesis

Amyloid fibrils form and precipitate in more than 50 incurable human diseases, including Alzheimer’s and Parkinson’s disease. All proteins may be able to form amyloids, at least under certain circumstances. However, aggregation is... ver más

30/04/2029

FUNDACIO INSTITUT...

2M€

Presupuesto del proyecto: 2M€

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FUNDACIO INSTITUT DE BIOENGINYERIA DE CATALUN... Otra investigación y desarrollo experimental en ciencias naturales y técnicas asociacion

TRL 4-5 | 50K€

Fecha límite participación Sin fecha límite de participación.

Financiación concedida El organismo HORIZON EUROPE notifico la concesión del proyecto el día 2024-02-14

ERC-2023-COG: ERC CONSOLIDATOR GRANTS Scope:Objectives

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1 Participantes

FUNDACIO INSTITUT DE BIOENGI...

2.00M€ | Lider

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Duración del proyecto: 62 meses Fecha Inicio: 2024-02-14
Fecha Fin: 2029-04-30

Líder del proyecto

FUNDACIO INSTITUT DE BIOENGINYERIA DE CATALUN... Otra investigación y desarrollo experimental en ciencias naturales y técnicas asociacion

TRL 4-5 | 50K€

Presupuesto del proyecto 2M€

Fecha límite de participación Sin fecha límite de participación.

Descripción del proyecto Amyloid fibrils form and precipitate in more than 50 incurable human diseases, including Alzheimer’s and Parkinson’s disease. All proteins may be able to form amyloids, at least under certain circumstances. However, aggregation is actually rare as the process of amyloid formation is controlled by a high kinetic barrier: protein sequences have to cross a free energy barrier to nucleate transition states which then seed irreversible fibril formation. Short-lived transition states are extremely challenging to study using biophysical methods. We have recently developed a massively parallel genomics approach to quantify the rate of aggregation of thousands of protein sequences. We also have evidence that, by quantifying the interactions between mutations, we can capture the key interactions between residues in the transition state. Here, we will unleash the potential of this approach by targeting the following aims: 1) Map the impact on amyloid nucleation of all possible mutations in >60 human and functional amyloids - generating reference atlases for clinical variant interpretation 2) Build an energetic and structural model of the transition state of disease-associated amyloids 3) Uncover sequences across the genome that nucleate amyloids in response to environmental stress This project will uncover the rules required to understand, predict and engineer amyloid formation. By identifying the mutations that do and do not lead to amyloid formation, we will reveal which variants accelerate aggregation and cause disease. We will also address one of the most important questions in the field, i.e. identifying the interactions established in the transition states of amyloid nucleation, guiding the development of therapeutic approaches in amyloid diseases, including the worst kinds of dementia. Finally, our results will feed a new generation of models and predictors of protein aggregation to employ for disease variant interpretation and the synthetic design of novel proteins.

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