Computing and Library Services - delivering an inspiring information environment

Investigating the mechanisms responsible for and the factors affecting protein aggregation

Fenton, Ami-Jane, Austerberry, James and Belton, Daniel J. (2012) Investigating the mechanisms responsible for and the factors affecting protein aggregation. In: Nanoformulation 2012, 27th May – 1st June 2012, Barcelona. (Unpublished)

Metadata only available from this repository.


Protein aggregation plays a huge role in developing new biomaterials and understanding the mechanisms responsible for a number of neurodegenerative diseases, including Alzheimer’s disease. The rate at which proteins aggregate and the way in which they aggregate is dependent on a variety of factors. Variations in conditions such as temperature, pH, protein concentration and the addition of metal ions such as zinc can affect whether the protein will form fibrils or particulates and how fast the aggregates will form. By understanding the mechanisms driving protein aggregation we can begin to investigate new techniques and drug systems for dealing with neurodegenerative disease as well as creating functional biomaterials using proteins. Here we present results gathered using light scattering spectroscopy and infrared analysis for several proteins where the conditions have been altered to either promote the formation of fibrils or particulate aggregates. This research will eventually give us important information about how to control protein aggregation and modify the mechanisms to produce an array of beneficial products including drugs and biological materials.

Item Type: Conference or Workshop Item (Poster)
Subjects: Q Science > QD Chemistry
Schools: School of Applied Sciences
Related URLs:
Depositing User: Daniel Belton
Date Deposited: 28 Aug 2014 11:41
Last Modified: 28 Aug 2021 11:41


Downloads per month over past year

Repository Staff Only: item control page

View Item View Item

University of Huddersfield, Queensgate, Huddersfield, HD1 3DH Copyright and Disclaimer All rights reserved ©