Effect of hydrophobic residues on amyloid formation under steady shear and at interfaces
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Authors
McBride, Samantha Ann
Issue Date
2015-08
Type
Electronic thesis
Thesis
Thesis
Language
ENG
Keywords
Chemical engineering
Alternative Title
Abstract
A surprisingly large number of proteins of different shapes, sizes, and functions are capable of undergoing fibrillization transformations in which protein monomers become unstable and begin to combine in a crystalline fashion to form long, thin structures, known as amyloid fibrils. Accumulation of amyloid fibrils leads to a number of disorders, including Alzheimer’s and Parkinson’s diseases. Shearing flows and hydrophobic interfaces are ubiquitous throughout the body and known to contribute strongly to fibrillization, yet the influence of these forces on amyloid formation are not well understood. Previous investigations regarding the effect of agitation on fibrillization kinetics have failed to reach a consensus on whether the effect is due to a simple increase in mixing, alterations of protein structure caused by shear extensional forces, or a combination of shear and hydrophobic interfaces.
Description
August 2015
School of Engineering
School of Engineering
Full Citation
Publisher
Rensselaer Polytechnic Institute, Troy, NY