Sewing machine inspires imaging tool for Alzheimer’s
21 Apr 2014 by Evoluted New Media
The humble sewing machine has inspired a new imaging tool which is providing new clues about the origins of Alzheimer’s and Parkinson’s disease. Ultrasonic Force Microscopy (UMF) was developed by physicist Dr Oleg Kolosov and his colleagues at Lancaster University to probe the toxic proteins characteristic of the disease, which are too small to be studied with traditional optical microscopy. “By using a vibrating scanner, which moves quickly up and down like the foot of a sewing machine needle, the friction between the sample and the scanner was reduced – resulting in a better quality, and high contrast nanometre scale resolution image,” said Kolosov. It was thought that Alzheimer’s was caused by the accumulation of long amyloid fibres at the centre of senile plaques because of improper folding of amyloid-?. However, this new research – published in Nature Scientific Reports – suggests that the fibres and plaques are actually the body’s protective response to smaller, more toxic structures made from amyloid-? called oligomers. UMF was used to image these oligomers; to see them more clearly, poly-L-lysine (PLL) was used to keep the proteins stuck to the slides as the scanner passed over them and to increase the contrast of the image. Biomedical scientist Professor David Allsop said: “The high quality images are vitally important if we are to understand the pathways involved in formation of these oligomers, and this new technique will now be used to test the effects of inhibitors of oligomer formation that we are developing as a possible new treatment for Alzheimer’s disease.” The technique worked so well that the team is hoping to develop it so that oligomer formation could be monitored in real time. This would give researchers a better understanding of the early phases of Alzheimer’s and Parkinson’s, and could offer a potential new way to develop tests for the disease. Ultrasonic force microscopy for nanomechanical characterization of early and late-stage amyloid-? peptide aggregation
