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| http://dx.doi.org/10.1371/journal.ppat.1002687 | DOI Listing |
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Synucleinopathies, including Parkinson's disease (PD), multiple system atrophy (MSA), and dementia with Lewy bodies (DLB), are neurodegenerative disorders caused by the accumulation of misfolded alpha-synuclein protein. Developing effective vaccines against synucleinopathies is challenging due to the difficulty of stimulating an immune-specific response against alpha-synuclein without causing harmful autoimmune reactions, selectively targeting only pathological forms of alpha-synuclein. Previous attempts using linear peptides and epitopes without control of the antigen structure failed in clinical trials.
View Article and Find Full Text PDFA Story Between s and S: [Het-s] Prion of the Fungus .
Mycobiology
March 2024
Department of Microbiology, Pusan National University, Busan, Korea.
In filamentous fungi, vegetative cell fusion occurs within and between individuals. These fusions of growing hyphae (anastomosis) from two individuals produce binucleated cells with mixed cytoplasm known as heterokaryons. The fate of heterokaryotic cells was genetically controlled with delicacy by specific loci named (heterokaryon) or (vegetative incompatibility) as a part of self-/nonself-recognition system.
View Article and Find Full Text PDFAnalytical Framework to Understand the Origins of Methyl Side-Chain Dynamics in Protein Assemblies.
J Am Chem Soc
March 2024
Institute for Medical Physics and Biophysics, Leipzig University, Härtelstraße 16-18, 04107 Leipzig, Germany.
Side-chain motions play an important role in understanding protein structure, dynamics, protein-protein, and protein-ligand interactions. However, our understanding of protein side-chain dynamics is currently limited by the lack of analytical tools. Here, we present a novel analytical framework employing experimental nuclear magnetic resonance (NMR) relaxation measurements at atomic resolution combined with molecular dynamics (MD) simulation to characterize with a high level of detail the methyl side-chain dynamics in insoluble protein assemblies, using amyloid fibrils formed by the prion HET-s.
View Article and Find Full Text PDFVaccination with structurally adapted fungal protein fibrils induces immunity to Parkinson's disease.
Brain
May 2024
Institut für Biologische Informationsprozesse, Strukturbiochemie (IBI-7), Forschungszentrum Jülich, 52425 Jülich, Germany.
The pathological misfolding and aggregation of soluble α-synuclein into toxic oligomers and insoluble amyloid fibrils causes Parkinson's disease, a progressive age-related neurodegenerative disease for which there is no cure. HET-s is a soluble fungal protein that can form assembled amyloid fibrils in its prion state. We engineered HET-s(218-298) to form four different fibrillar vaccine candidates, each displaying a specific conformational epitope present on the surface of α-synuclein fibrils.
View Article and Find Full Text PDFSERS probing of fungal HET-s fibrils formed at neutral and acidic pH conditions.
Spectrochim Acta A Mol Biomol Spectrosc
March 2024
Department of Electrical and Computer Engineering, University of Alberta, Edmonton T6G 1H9, AB, Canada. Electronic address:
Advances in precision medical diagnostics require accurate and sensitive characterization of pathogens. In particular, health conditions associated with protein misfolding require an identification of proteinaceous amyloid fibrils or their precursors. These pathogenic entities express specific molecular structures, which require ultra-sensitive, molecular-level detection methods.
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