ArticleFrontiers in neuroscience2017
Conformational Ensembles of α-Synuclein Derived Peptide with Different Osmolytes from Temperature Replica Exchange Sampling.
Article in Frontiers in neuroscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Proteoform-Resolved Cross-Linking Reveals Environment-Dependent Structural Effects of α-Synuclein S129 Phosphorylation.Journal of the American Chemical Society · 2026Article
- Beyond the structure-function paradigm: A comprehensive review of intrinsically disordered proteins.Biochemistry and biophysics reports · 2026Review
- Interactions Between Nutraceuticals and α-Synuclein Conformational States: Molecular Mechanisms and Neuroprotective Implications in Parkinson's Disease.International journal of molecular sciences · 2026Review
- The role of trimethylamine N-oxide in disease pathogenesis and the therapeutic potential of traditional Chinese medicine.Frontiers in pharmacology · 2025Review
- Application of temperature replica exchange molecular dynamics: Structure of mitotic spindle-associated protein SHE1 and its binding to dynein.Computational and structural biotechnology journal · 2025Article
- α-synuclein overexpression and the microbiome shape the gut and brain metabolome in mice.NPJ Parkinson's disease · 2024Article
- The Brain-Gut Axis, an Important Player in Alzheimer and Parkinson Disease: A Narrative Review.Journal of clinical medicine · 2024Review
- α-Synuclein Overexpression and the Microbiome Shape the Gut and Brain Metabolome in Mice.bioRxiv : the preprint server for biology · 2024Article
- Advanced computational approaches to understand protein aggregation.Biophysics reviews · 2024Review
- Gut Microbiota in Autophagy Regulation: New Therapeutic Perspective in Neurodegeneration.Life (Basel, Switzerland) · 2023Review
- Trimethylamine N-oxide: role in cell senescence and age-related diseases.European journal of nutrition · 2023Review
- Aggregation of a Parkinson's Disease-Related Peptide: When Does Urea Weaken Hydrophobic Interactions?ACS chemical neuroscience · 2022Article
- The relationship between Parkinson's disease and gastrointestinal diseases.Frontiers in aging neuroscience · 2022Review
- Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy.RSC chemical biology · 2021Article
- Ameliorating amyloid aggregation through osmolytes as a probable therapeutic molecule against Alzheimer's disease and type 2 diabetes.RSC advances · 2020Article
- Implication of Trimethylamine N-Oxide (TMAO) in Disease: Potential Biomarker or New Therapeutic Target.Nutrients · 2018Review
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered proteins (IDP) are a class of proteins that do not have a stable three-dimensional structure and can adopt a range of conformations playing various vital functional role. Alpha-synuclein is one such IDP which can aggregate into toxic protofibrils and has been associated largely with Parkinson's disease (PD) along with other neurodegenerative diseases. Osmolytes are small organic compounds that can alter the environment around the proteins by acting as denaturants or protectants for the proteins. In the present study, we have conducted a series of replica exchange molecular dynamics simulations to explore the role of osmolytes, urea which is a denaturant and TMAO (trimethylamine N-oxide), a protecting osmolyte, in aggregation and conformations of the synuclein peptide. We observed that both the osmolytes have significantly distinct impacts on the peptide and led to transitions of the conformations of the peptide from one state to other. Our findings highlighted that urea attenuated peptide aggregation and resulted in the formation of extended peptide structures whereas TMAO led to compact and folded forms of the peptide.
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