Research Paper on Physiologic States, Pathologic Strains, and Biotechnological Applications of -Synuclein Conformational Plasticity

Description

Title: Physiologic States, Pathologic Strains, and Biotechnological Applications of -Synuclein Conformational Plasticity

Abstract: Both its extensive conformational plasticity and its pathological prion-like characteristics make -synuclein (S) noteworthy. Biologically, S can be found in oligomeric states bound to membranes, helically folded tetrameric states, or disordered monomeric states. Pathologically, S may form harmful oligomers and then fibrils. This prion-like transmission is thought to be responsible for a group of neurodegenerative diseases known as -synucleinopathies. Notably, S exists as structurally different amyloid-like conformations known as “strains,” rather than adopting a single “amyloid fold”. Animal models that have been vaccinated with various strains develop different pathologies, and new research indicates that the different pathologies seen in patients with various -synucleinopathies are caused by the spread of disease-specific strains. The structural underpinnings of Parkinson’s disease, multiple system atrophy, and dementia with Lewy bodies have been revealed through the characterization of S strains. In this review, we first examine the physiological and pathological variations among the states of S’s con-formation. The impact of microenvironmental factors on the emergence, spread, and pathological traits of the S species is then covered in recent research. Finally, we discuss how knowledge of S conformational properties has been applied to new strain amplification techniques, which have shed more light on the function of particular strains in various -synucleinopathies and hold promise for disease early diagnosis.

Keywords: α-synuclein; tetramer; α-synucleinopathy; prion-like; strains; PMCA; RT-QuIC

Paper Quality: SCOPUS / Web of Science Level Research Paper

Subject: Biomolecules

Writer Experience: 20+ Years

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