Description
Title: A chameleon in the gear: Synuclein Fibrils as Penrose Machines
Abstract: Lionel Penrose created the first mechanical self-replicating device in 1957 and demonstrated its operation in a number of machine prototypes, foreshadowing our current understanding of the origin and spread of amyloid fibrils. With the aid of his son Roger, he created and demonstrated the ideas that would, decades later, form the cornerstones of the study of prion and prion-like neurobiology, including the concepts of nucleation, seeding, and conformational templating of monomers, linear polymer elongation, fragmentation, and spread. He publicly presented his premonitory discovery in a film, which we have reproduced here, at just two conferences in 1958. By jumping forward 30 years to the early 1990s, we recall the studies conducted by Peter Lansbury and his team in which -Synuclein (-Syn) was first I compared to a prion, (ii) demonstrated to contain a fibrillization-prone domain capable of seeding its own assembly into fibrils, (iii) identified as an intrinsically disordered protein (IDP), and (iv) described by one of us as a We suggest that the emergence and spread of a variety of -Syn fibril strains in -Synucleinopathies, a phenomenon that is currently of interest, can be adequately explained by the combination of the chameleon nature of -Syn with the rigid gear of the Penrose machine.
Keywords: α-Synuclein; amyloid; fibril; strain; intrinsically disordered protein; Parkinson’s disease; prion; PrP; sup35; seeding; templating; self-replication
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Biomolecules
Writer Experience: 20+ Years
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