Novel Use of SPR to Study Amyloidogenic Peptides and Proteins

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March 16, 2017

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  • "For more info, visit http://www.bio-rad.com/yt/4/ProteinInteraction. An increasing number of diseases are now being associated with misfolding, aggregation, and tissue deposition of specific proteins. A well-known example is Alzheimer's disease (AD). The condition is characterized by the aggregation of β-amyloid peptides (Aβ1–40 and Aβ1–42), which form amyloid plaques. The plaques are mainly composed of insoluble Aβ fibrils formed by fibrillogenesis. However, recent evidence suggests a pathogenic role for soluble oligomers appearing early in the fibrillogenesis process. This webinar will illustrate unconventional applications of surface plasmon resonance (SPR) to measure the kinetics of the elongation of Aβ1–42 fibrils and recognize soluble Aβ1–42 oligomeric species, which cannot be achieved by other techniques. These approaches are very useful in screening mutations or potential anti-amyloidogenic drugs for their effects on fibrillogenesis and the formation of toxic oligomers. Presenter: Marco Gobbi Head, Laboratory of Pharmacodynamics and Pharmacokinetics Istituto di Ricerche Farmacologiche Mario Negri Milano Italy http://www.bio-rad.com/evportal/destination/solutions?catID=LUSLTJE8Z&WT.mc_id=yt-pfd-ww-proteon-20120912-ziw-bMeUzNc"

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