In this webinar you will learn:
- How Microfluidic Modulation Spectroscopy (the AQS3pro) allows users to ‘see change’ in the secondary structure of proteins across a wide concentration range from 0.1 to over 200 mg/ml, and in the presence of excipients.
- How synthetic alpha sheets could form the basis of therapeutics to clear toxic oligomers in people.
- How ongoing studies are extending this research to other amyloid disease systems.
Amyloid Beta Protein Aggregation
Amyloid beta proteins are formed by neurons in the brain, where they perform important task include protecting the body from infections, repairing leaks in the blood-brain barrier, and regulating synaptic function. Aggregates of misfolded Amyloid beta, known as plaques, are strongly associated with diseases such as Alzheimer’s and Creutzfeldt Jakob Syndrome.
These plaques were long believed to trigger the cognitive impairments in Alzheimer’s disease, however recent research implicates smaller aggregates (oligomers) of amyloid beta as the toxic elements of this disease.
Monitoring Alpha Sheet Secondary Structure
Prof. Valerie Daggett and her team at the University of Washington developed synthetic peptides to target and inhibit these small, toxic aggregates. They designed these peptides to fold into a structure called an alpha sheet that can block amyloid beta aggregation at the early and most toxic stage when oligomers form.
In this webcast, Daggett and team describe how using the Microfluidic Modulation Spectroscopy-based AQS3pro (RedShiftBio) they observed all stages of amyloid beta cluster development. The research was able to identify monomers to six- and 12-protein oligomers, to plaques-- giving an unprecedented view of this alpha-sheet structure both in their synthesized peptides and in toxic species of amyloid beta.
The webinar featured a lively Q&A session. Below are some of the questions that were asked. Register to see the full transcript of the questions and answers
Are there any buffers, typically found in protein formulations, that are incompatible with Microfluidic Modulation Spectroscopy?
Is there any water vapor subtraction applied to the MMS?