Signal peptide region of SAA1: misfolding propensity in different animal species

dc.contributor.authorBurke, Pierce M.
dc.date.accessioned2022-05-02T13:16:07Z
dc.date.available2022-05-02T13:16:07Z
dc.date.issued2022
dc.description1 Broadside. 48"W x 36"Hen_US
dc.description.abstractIn AA 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, inflammatory bowel disease, and rheumatoid arthritis. It has been hypothesized that certain regions of the protein have a higher propensity to misfold, and this study particularly focuses on the signal peptide region of SAA. A library of peptides from both domestic and wild animals was used to study aggregation propensity via in silico analysis and in vitro assays. It was found that each peptide aggregated in the given conditions of the experiment. This suggests that further research in the signal peptide region may provide future therapeutic strategies for amyloidosis.en_US
dc.description.sponsorshipKalamazoo College. Department of Biology. Diebold Symposium, 2022en_US
dc.format.mimetypeapplication/pdf
dc.identifier.urihttps://cache.kzoo.edu/handle/10920/43560
dc.language.isoen_USen_US
dc.publisherKalamazoo, Mich. : Kalamazoo Collegeen_US
dc.relation.ispartofKalamazoo College Diebold Symposium Presentation Collectionen
dc.rightsU.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder.en
dc.titleSignal peptide region of SAA1: misfolding propensity in different animal speciesen_US
dc.typePresentationen_US
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