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Nanomaterial, protein, amyloid, functionalization, fibril, nanofiber They are considered the core pathological markers of different neurodegenerative diseases The accumulation of abnormal protein fibrillar aggregates is a hallmark of various neurodegenerative diseases
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Notably, a single type of protein species can form fibrils with distinct morphologies, and recent studies have linked fibril polymorphism to variations in disease symptoms Amyloid fibrils are one of the important forms of protein aggregates, first discovered in the pathological brain tissues of patients with various neurodegenerative diseases However, the mechanisms underlying the formation and structural distinction of these morphologies remain elusive.
It is primarily produced by the liver in response to proinflammatory cytokines during acute inflammation [3].
Introduction amyloid fibrils are formed by normally soluble proteins, which assemble to form insoluble fibers that are resistant to degradation Their formation can accompany disease and each disease is characterized by a specfic protein or peptide that aggregates. Despite their structural similarities, amyloid fibrils formed by different proteins, or even by the same protein under different conditions, can vary considerably in internal structure and biological effects This phenomenon, known as fibril polymorphism, is a key feature of amyloid biology [4,5]
Amyloid fibrils are highly stable misfolded protein assemblies that play an important role in several neurodegenerative and systemic diseases Although structural information of the amyloid state.
