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Study of amyloid formation and inhibition by ion mobility-mass spectrometry (CAT#: STEM-ST-0161-LJX)

Introduction

Amyloidogenic peptide oligomers are responsible for a variety of neurodegenerative disorders such as Alzheimer’s and Parkinson’s disease. Due to their dynamic, polydisperse, and polymorphic nature, these oligomers are very challenging to characterize using traditional condensed-phase methods. In the last decade, ion mobility-mass spectrometry (IM-MS) and related gas-phase techniques have emerged as a powerful alternative to disentangle the structure and assembly characteristics of amyloid forming systems. This review highlights recent advances in which IM-MS was used to characterize amyloid oligomers and their underlying assembly pathway.




Principle

Ion mobility spectrometry–mass spectrometry (IMS-MS) is an analytical chemistry method that separates gas phase ions based on their interaction with a collision gas and their masses. In the first step, the ions are separated according to their mobility through a buffer gas on a millisecond timescale using an ion mobility spectrometer. The separated ions are then introduced into a mass analyzer in a second step where their mass-to-charge ratios can be determined on a microsecond timescale.

Applications

For studying the gas phase ion structure
For detecting the chemical warfare agents and explosives
For the analysis of proteins, peptides, drug-like molecules and nano particles
For monitoring isomeric reaction intermediates and probe their kinetics
For proteomics and pharmaceutical analysis

Procedure

1. Add sample
2. The ions in the sample are separated in the ion mobility spectrometer
3. The separated ions are introduced into the mass analyzer for detection
4. Store the detection results

Materials

• Sample Type:
Amyloid

Notes

1. Ion mobility spectrometry is also a very fast technique, making it suitable for high-throughput applications. The entire analysis can be completed in just a few minutes.
2. The method is extremely sensitive and able to detect trace amounts of contaminants that other spectrometry methods would miss.
3. The effective separation of analytes achieved with this method makes it widely applicable in the analysis of complex samples such as in proteomics and metabolomics.
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