Novel Application of SPR to Study Amyloidogenic Peptides and Proteins




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Published on Jul 23, 2012

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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 illustrates 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.

Marco Gobbi
Head, Laboratory of Pharmacodynamics and Pharmacokinetics
Istituto di Ricerche Farmacologiche Mario Negri


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