Amyloid Fibrils, Spherulites and Beyond: Unravelling Mechanisms that Control Protein Aggregation

Lead Research Organisation: University of Nottingham
Department Name: Sch of Physics & Astronomy

Abstract

Abstracts are not currently available in GtR for all funded research. This is normally because the abstract was not required at the time of proposal submission, but may be because it included sensitive information such as personal details.

Publications

10 25 50
publication icon
Bailey J (2010) Thin film polymer photonics: Spin cast distributed Bragg reflectors and chirped polymer structures. in The European physical journal. E, Soft matter

publication icon
Farmer D (2013) Quantized phonon modes in loaded polymer films in Journal of Applied Physics

publication icon
Foderà V (2012) Microfluidics Reveals a Flow-Induced Large-Scale Polymorphism of Protein Aggregates in The Journal of Physical Chemistry Letters

publication icon
Langley KR (2010) Microtextured surfaces with gradient wetting properties. in Langmuir : the ACS journal of surfaces and colloids

publication icon
Sharp JS (2011) Contact angle dependence of the resonant frequency of sessile water droplets. in Langmuir : the ACS journal of surfaces and colloids

publication icon
Smith MI (2014) Origin of contact line forces during the retraction of dilute polymer solution drops. in Langmuir : the ACS journal of surfaces and colloids

 
Description This project has shown that environmental factors such as pH, temperature and protein concentration influence the balance between amyloids fibrils and spherulites druing the aggregation of proteins. In particular we have shown that the size and number of spherulites formed is sensitive to pH and temperature. The observed behaviour has been interpreted in terms of the colloidal and conformational stability of proteins.

Under certain conditions it is possible to form giant amyloid spherulites which have diameters as large as 1mm. When viewed under cross polarisers these aggregates display a rich variety of colours or isochromes. We have developed a theoretical model which allows us to predict the shapes of the isochromes that form and to obtain information about the internal structure of the protein aggregates.

In addition, we have also developed a simple processing based method for the manufacture of organic photonic structures. We have performed detailed measurements of crack pattern formation in thin colloidal films. We have also derived a theory which explains how the confining influence of a substrate influences these patterns.

Studies of droplet vibration have also allowed us to develop a technique for measuring the surface tension and viscosity of small liquid volumes.
Exploitation Route Understanding how environmental factors influence the final morphology of protein aggregates is important in determining how to treat diseases such as Alzheimer's and Parkinson's disease. Studies of the structural properties of amyloid spherulites are also important for extracting information about the molecular level assembly processes that take place during the formation of these harmful aggregates. These studies will therefore act to inform researchers and health care professionals so that a better understanding of protein aggregation can be obtained by the wider scientific community.



Solution processed polymer based photonic structures offer low cost alternatives to inorganic devices. They are also manufactured using less toxic materials. Plastic photonics will be useful in the manufacture of low cost organic optoelectronic devices such as solar cells and light emitting diodes.
Sectors Energy,Healthcare

 
Description To inform further studies of relaxations in thin polymer films
First Year Of Impact 2000
Sector Other
Impact Types Societal