What is the exact mechanism by which the protein folding process occurs and how can misfolded proteins lead to various neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's?
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During protein folding, a complex and dynamic process, polypeptide chains adopt their three-dimensional structures. The primary driving forces behind protein folding are hydrophobic interactions, electrostatic interactions, hydrogen bonding, and van der Waals forces. Chaperone proteins also assist in ensuring correct folding.
Misfolded proteins can have detrimental effects on cellular function. In neurodegenerative diseases like Alzheimer's, Parkinson's, and Huntington's, specific proteins (amyloid-beta, alpha-synuclein, and huntingtin, respectively) misfold and aggregate, forming toxic clumps. These aggregates can disrupt cellular processes, interfere with protein degradation pathways, and lead to the formation of inclusion bodies.
The accumulation of misfolded proteins contributes to the formation of neurotoxic oligomers and fibrils, causing cellular dysfunction and neuronal death. Additionally, these protein aggregates can induce inflammation, oxidative stress, and impair synaptic function. The exact mechanisms through which misfolded proteins cause neurodegenerative diseases are complex and not yet fully understood, but the resulting protein aggregation and cellular dysfunction play crucial roles in disease progression.
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