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Digital Protein Biophysics of Aggregation

Project description

How protein clusters form

Proteins, the fundamental building blocks of life, bind together to form functional complexes. However, in certain cases, they can form aberrant complexes that have dramatic consequences for biological systems and are implicated in neurodegenerative disorders. Conventional approaches to understanding the formation of protein clusters have been challenging as the formation of protein clusters results in aggregates of different sizes and properties and correspondingly diverse effects on the function of living cells. The EU-funded DiProPhys project will address this challenge through a combination of microfluidics and single-molecule spectroscopy, creating a novel digital biophysics platform for studying protein aggregation. Using this approach, DiProPhys will be able to study aggregates one by one, inside and outside cells, and discover the fundamental physical factors that govern their formation and effects on the cellular systems.

Objective

Proteins are the fundamental building blocks of life, underpinning functional processes in living systems. They are able to exert their biological activities by binding to other proteins to form functional complexes which act as the machinery of life. In certain cases, however, proteins escape cellular quality control mechanisms and form aberrant complexes. The formation of such clusters stabilised by inter-molecular hydrogen bonds, amyloid aggregates, has dramatic consequences for biological systems and they are implicated in neurodegenerative disorders. The fundamental biophysical chemistry governing the formation of protein clusters has been challenging to probe and understand as this process results in a highly heterogeneous distribution of aggregates of different sizes and with different properties, and correspondingly diverse effects on living cells’ function. As such, conventional bulk methods are challenging to apply to uncover a fundamental biophysical understanding of their formation, dynamics and behaviour. The present proposal addresses this fundamental problem by bringing together microfluidics and single molecule spectroscopy to develop a novel digital biophysics platform for studying protein aggregation. Through this route, we will be able to study aggregates one by one, inside and outside cells, and discover the fundamental physical determinants that govern their formation and effects on the cellular systems. This proposal is motivated by the hypothesis that the physico-chemical properties of protein aggregates modulate their biological activity, and by studying protein aggregation at the level of single aggregates and single cells, we will access fundamentally new biophysical chemistry, including how liquid-liquid phase separation can modulate the nucleation barriers in protein aggregation, what the molecular mechanisms are by which amyloid aggregates can self-multiply, and what physical parameters determine their effects on living cells.

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Keywords

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Programme(s)

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Topic(s)

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Funding Scheme

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ERC-COG - Consolidator Grant

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Call for proposal

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(opens in new window) ERC-2020-COG

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Host institution

THE CHANCELLOR MASTERS AND SCHOLARS OF THE UNIVERSITY OF CAMBRIDGE
Net EU contribution

Net EU financial contribution. The sum of money that the participant receives, deducted by the EU contribution to its linked third party. It considers the distribution of the EU financial contribution between direct beneficiaries of the project and other types of participants, like third-party participants.

€ 1 999 715,00
Address
TRINITY LANE THE OLD SCHOOLS
CB2 1TN CAMBRIDGE
United Kingdom

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Region
East of England East Anglia Cambridgeshire CC
Activity type
Higher or Secondary Education Establishments
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Total cost

The total costs incurred by this organisation to participate in the project, including direct and indirect costs. This amount is a subset of the overall project budget.

€ 1 999 715,00

Beneficiaries (1)

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