Villigen - Researchers from the Paul Scherrer Institute (PSI) are looking into the possibilities of breaking down protein structures that cause neurodegenerative diseases. One option could potentially involve the use of spermine to eliminate nerve-damaging deposits.
(CONNECT) A team of researchers led by Jinghui Luo from the Center for Life Sciences at the Paul Scherrer Institute (PSI) is investigating ways to eliminate damaging protein deposits in the brain that are seen as being responsible for neurodegenerative diseases such as Alzheimer’s and Parkinson’s. According to a press release issued by PSI, which is based in Villigen in the Swiss canton of Aargau, the polyamine spermine is being considered as a possible option for this.
In the course of their investigations, the researchers discovered that incorrectly folded protein structures, known as amyloid proteins, accumulate in the aging brain. The body’s own spermine - named after seminal fluid, where this polyamine is found in high concentrations - is able to break down and eliminate these nerve-damaging deposits. At the same time, spermine has the ability to strengthen the mitochondria, which are considered to be the powerhouses of the cells.
Luo’s group obtained their research results using optical microscopy and the SAXS scattering technique at PSI’s own Swiss Light Source (SLS). The nematode C. elegans served as a model organism, allowing the biochemical mechanism to be explained. It was shown that spermine causes the harmful proteins to accumulate and clump together through biomolecular condensation. These proteins are encapsulated in small membrane vesicles and ultimately degraded through a process known as autophagy, which regularly occurs in human cells. “Autophagy is more effective at handling larger protein clumps”, as study leader Luo explains, adding that: “And spermine is, so to speak, the binding agent that brings the strands together. There are only weakly attractive electrical forces between the molecules, and these organize them but do not firmly bind them together”.
Attention will now turn to investigating whether other polyamines can perform these functions. The study has been published in the latest edition of the journal Nature Communications. ce/ww
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