News

A computational suite for the structural and functional characterization of amyloid aggregates

Researchers from the University of Cambridge have unveiled a computational suite designed for the structural and functional characterization of amyloid aggregates. According to experts, amyloid aggregation is a hallmark of several degenerative diseases affecting the brain or peripheral tissues, whose intermediates (oligomers, protofibrils) and final mature fibrils display different toxicity (Protein folding and aggregation into amyloid).

The newly developed tool called Amyloid Characterization Toolkit (ACT) automates the analysis of fluorescence microscopy images, providing precise counting and characterization of amyloid aggregates. For the imaging setup, the scientists employed the used of our Cobolt Jive™ 561nm and our Cobolt 06-MLD 638 nm lasers. With a 90% counting accuracy and rapid processing capabilities, ACT promises to streamline research on amyloid diseases and protein aggregation.

Significance of the study:

This toolkit enhances the ability of researchers to study the formation, structure, and function of amyloid aggregates, providing valuable insights into their role in neurodegenerative diseases. By facilitating more accurate and efficient analysis, ACT can contribute to the development of new therapeutic strategies for conditions like Alzheimer’s disease.

Super-resolution Imaging Unveils the Self-replication of Tau Aggregates Upon Seeding

Dementia is one of the major causes of disability among older people affecting 50 million people worldwide. Alzheimer’s disease (AD) is the most common form of dementia, characterized by extensive neuronal loss and severe brain shrinkage. As experts have noted, this pathology is driven by the accumulation of extracellular amyloid-beta (Ab) plaques and intracellular hyperphosphorylated tau aggregates. As it turns out, in Alzheimer’s disease, an abnormal form of tau accumulates and begins sticking together in thread-like structures called neurofibrillary tangles. These tangles are not effectively disposed of through the cell’s usual ways of removing “trash.” As a result of this build-up the microtubule superhighway becomes damaged, thus disrupting the normal functions of neurons (Tau protein in Alzheimer’s disease).

Researchers from the University of Cambridge have made significant strides in understanding Alzheimer’s disease by using super-resolution microscopy to observe tau protein aggregates within cells with the help of the Cobolt 06-MLD. The group used the following wavelengths: 405, 488, 561 and 638 nm.

For the first time, scientists are able to visualise how tau aggregates form and replicate. Their study highlights that even without external seeding, cells can spontaneously form small tau aggregates.

Significance of the study:

The research is significant as it clarifies how tau aggregates replicate themselves, which helps advance our knowledge on the mechanisms behind neurodegenerative disease such as Alzheimer’s. Researchers will be able to harness this information for early detection and diagnosis to empower earlier treatment and better patient outcomes for the future.