Signal peptide region of SAA1 : misfolding propensity in different animal species
Loading...
Authors
Burke, Pierce M.
Issue Date
2022-01-01
Type
Thesis
Language
en_US
Keywords
Alternative Title
Abstract
In amyloidosis, fibrils are formed from the misfolding of fragmented serum amyloid A (SAA) protein. These fibrils aggregate in tissues, causing diseases such as Alzheimer’s, Type II diabetes, prion diseases, and chronic inflammatory disease. It has been hypothesized that certain regions of the protein have a higher propensity to misfold, and this study will particularly focus on the signal peptide region of SAA. The SAA protein was fragmented and sequenced. A library of 35 peptides (fragments 1-19) from both domestic and wild animals was used to study aggregation propensity via in silico analysis and in vitro assays. After running an in-silico analysis as well as transmission electron microscopy, Congo red binding assay, and finally a ThT fluorescence assay, it was determined that each peptide aggregated in the given conditions of the experiment. With all peptides aggregating, that means the signal peptide region may play a role in amyloidogensis. This data points to the idea that further research in the signal peptide region can potentially play a role in future therapeutic strategies for amyloidosis.
Description
v, 21 p.
Citation
Publisher
Kalamazoo College
License
U.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder.