Fibrillenvorming

Fibrillenvorming refers to the process by which individual protein molecules aggregate and align to form larger, insoluble filamentous structures called fibrils. This process is a key characteristic of several significant biological phenomena, including the formation of amyloid deposits in neurodegenerative diseases and the structural organization of proteins within cells. Fibrillenvorming is often driven by specific intermolecular interactions, such as hydrogen bonds and hydrophobic interactions, which stabilize the extended, ordered arrangement of the protein chains.

The formation of fibrils can be a spontaneous process under certain conditions, such as changes in pH, temperature, or concentration of the protein. In some cases, it can be influenced by the presence of pre-existing fibril seeds, accelerating the process through a phenomenon known as nucleation-dependent polymerization. While fibril formation is central to the pathology of diseases like Alzheimer's and Parkinson's, where misfolded proteins aggregate into toxic amyloid fibrils, it also plays crucial roles in normal cellular functions, such as the formation of cytoskeletal elements like actin filaments and microtubules. Understanding the mechanisms of fibrillenvorming is vital for developing therapeutic strategies for diseases associated with aberrant protein aggregation and for harnessing the structural properties of fibrils for biotechnological applications.