Event Title
Blocking the Aggregation of the Sup35 Prion Using Natural Extracts
Faculty Mentor
Michael Gleason
Keywords
Michael Gleason
Abstract
An inherently disordered protein (IDP) is a protein that easily refolds from a normal cellular conformation into an amyloidogenic conformation that leads to its aggregation into a fiber called an amyloid. Prions are amyloids that are additionally infectious. Sup35 is a yeast IDP that normally functions in translation termination and as an amyloid its a model in the study of amyloid physiology and pathology involved in Alzheimer’s and Parkinson’s Diseases, and others diseases like the rare variant-Creutzfeldt-Jacob Disease (human form of mad cow disease). We have expressed and isolated the amyloidogenic portion of the yeast Sup35 proten (Sup35NM) and have begun to compare the kinetics of aggregation alone and in the presence of various natural extracts that may block amyloidogenesis. These in vitro experiments are monitored using thioflavin T which fluoresces in the presence of aggregated proteins.
Session Name:
Poster Presentation Session #2 - Poster #20
Start Date
4-4-2014 12:15 PM
End Date
4-4-2014 1:00 PM
Location
HSB 3rd Floor Student Commons
Blocking the Aggregation of the Sup35 Prion Using Natural Extracts
HSB 3rd Floor Student Commons
An inherently disordered protein (IDP) is a protein that easily refolds from a normal cellular conformation into an amyloidogenic conformation that leads to its aggregation into a fiber called an amyloid. Prions are amyloids that are additionally infectious. Sup35 is a yeast IDP that normally functions in translation termination and as an amyloid its a model in the study of amyloid physiology and pathology involved in Alzheimer’s and Parkinson’s Diseases, and others diseases like the rare variant-Creutzfeldt-Jacob Disease (human form of mad cow disease). We have expressed and isolated the amyloidogenic portion of the yeast Sup35 proten (Sup35NM) and have begun to compare the kinetics of aggregation alone and in the presence of various natural extracts that may block amyloidogenesis. These in vitro experiments are monitored using thioflavin T which fluoresces in the presence of aggregated proteins.