Toxic Protein Accumulation Causes Nerve Damage in Parkinson’s Disease

Parkinson’s disease is a neurological illness that causes tremors, slow movement, and joint stiffness and can lead to significant cognitive impairments. It has a high global prevalence. The occurrence of Parkinson’s may rise as people live longer lives. The illness can cause movement abnormalities and several psychological and physiological issues.

Illustration Showing How α-Syn monomers Form Aggregates Inside Neurons Inducing Cell Toxicity

Illustration Showing How α-Syn monomers Form Aggregates Inside Neurons Inducing Cell Toxicity. Credit: Nature Neuroscience

Read Also: Hearing Loss and Epilepsy May Be Early Symptoms of Parkinson’s Disease Study Shows

Parkinson’s disease occurs due to the death of neurons in some brain areas. A protein known as alpha-synuclein misfolds and joins together into damaging aggregates in afflicted nerve cells. The mechanics behind the cause of the protein pathology are not fully understood. The scientists in this new study created a new sensitive way of studying what occurs to alpha-synuclein throughout the early stages of sickness. The scientists discovered how an accumulation of toxic protein begins within nerve cells in Parkinson’s disease, eventually leading to neuronal cell death. The study gives fresh insight into a critical physiological mechanism underlying Parkinson’s disease by investigating how, where, and why this build-up occurs.

A new explanation for nerve injury in Parkinson’s disease

The exact method of how Parkinson’s disease occur has been elusive to scientists for years. These limitations have prevented a better understanding of the illness and ways to address therapy.

The present research comprised a multi-team of scientists. The research team of neurologists, chemists, and structural biologists discovered that alpha-synuclein interacts with the membranes, or linings, of structures within neuronal cells. When it comes into contact with the membrane wall of the mitochondria, the part of the cell involved in energy production, it causes alpha-synuclein to misfold and clump.

The protein joins then accumulate heavily on the surface of the mitochondria, causing damage to the surface, causing holes to form on the membrane, and interfering with the mitochondria’s ability to generate energy. These changes cause the mitochondria to release signals that cause the nerves to die. While there are several types of Parkinson’s disease, this protein is known to misfold and join together in various forms. However, these misfolded proteins are cleaned and eliminated from the cell while neurons are healthy. The elimination process of this dangerous protein slows down as people age. The scientists hope to continue investigating how protein pathology inside cells impacts cell function and health.

Read Also: A Peptide Modified by UK Scientists Could Cure Parkinson’s Disease

Clinical significance

Parkinson’s disease is one of the most common movement illnesses globally. The disorder is incurable and progressing. The current study approach might potentially analyze how proteins misfold in other neurodegenerative illnesses. Using this new technique, scientists may test novel medicines to reduce protein misfolding and determine if these therapies may restore health to a damaged cell.


Although much progress has been made in understanding protein misfolding, the vital issue has been to examine the early phases of this process inside the human cell. The latest work sheds light on what happens in the early periods of protein misfolding and how it affects the health of the cell. These add to our understanding of the biochemical pathways behind Parkinson’s disease.

Read Also: Two Amino Acids Administered Intranasally Could Cure Parkinson’s Disease


Pathological structural conversion of α-synuclein at the mitochondria induces neuronal toxicity



Want to Stay Informed?

Join the Gilmore Health News Newsletter!

Want to live your best life?

Get the Gilmore Health Weekly newsletter for health tips, wellness updates and more.

By clicking "Subscribe," I agree to the Gilmore Health and . I also agree to receive emails from Gilmore Health and I understand that I may opt out of Gilmore Health subscriptions at any time.