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Characterizing Amyloid-Forming Immunoglobulin G Light and Variable Chains Using Microfluidic Modulation Spectroscopy
A deeper structural dive into light chain amyloidosis.

Protein structure is vitally important to function, however, loss in activity is not the only misfortune for misfolded proteins as they can also be immunogenic and disease-causing as in the case of amyloid plaques. Light chain amyloidosis results from the aggregation of the light chain in Immunoglobulin G (IgG) which is one of the most prevalent proteins in human serum.

In this webinar, we will cover the structural analysis of both light and variable chain domains of non-disease-causing IgGs from germline (GL), potential disease-causing domains from patients with multiple myeloma (MM), and disease-causing domains from amyloidosis patients (AL). Each sample was analyzed using Microfluidic Modulation Spectroscopy (MMS), a high-precision secondary structure characterization tool developed by RedShiftBio. Full Structural Characterization of IgG is important because the mechanism of aggregation is still unknown and further elucidation could lead to insights into potential treatments and cures.

Aug 23, 2022 10:00 AM in Eastern Time (US and Canada)

RedShiftBioⓇ is a forward-thinking technology company providing a powerful,  life sciences platform for reliable and accurate detection of pivotal changes in molecular structure that affect the critical quality attributes governing the safety, efficacy, an
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Speakers

Valerie Collins, PhD
Applications Manager @RedShiftBio
Valerie Collins, Ph.D. is the Applications Manager at RedShiftBio. She was involved in one of the first Beta tests for the AQS3pro while in graduate school at Clark University in Worcester, MA. In graduate school, Valerie worked in a Biophysical Chemistry lab gaining experience in protein expression and purification, CD, NMR, fluorescence spectroscopy, mass spectrometry, transmission electron microscopy, and computer simulations in order to address new ways of detecting, inhibiting, and degrading amyloid assemblies.