ArticleJournal of molecular biology2009
Examining polyglutamine peptide length: a connection between collapsed conformations and increased aggregation.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 142 citations in OpenAlex.
- Multiscale Simulations Elucidate the Mechanism of Polyglutamine Aggregation and the Role of Flanking Domains in Fibril Polymorphism.The journal of physical chemistry. B · 2025Article
- Impact of Glycoclustering on Stiffening of MUC5AC Peptides Revealed by High-Efficiency Synthesis.Angewandte Chemie (International ed. in English) · 2025Article
- Intrinsic stiffness andPNAS nexus · 2025Article
- Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations.JACS Au · 2024Article
- Tracing the Evolutionary History of the Temperature-Sensing Prion-like Domain in EARLY FLOWERING 3 Highlights the Uniqueness of AtELF3.Molecular biology and evolution · 2024Article
- Article
- Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022Review
- Template-assisted design of monomeric polyQ models to unravel the unique role of glutamine side chains in disease-related aggregation.Chemical science · 2021Article
- Connecting Coil-to-Globule Transitions to Full Phase Diagrams for Intrinsically Disordered Proteins.Biophysical journal · 2020Article
- Physical Chemistry of the Protein Backbone: Enabling the Mechanisms of Intrinsic Protein Disorder.The journal of physical chemistry. B · 2020Review
- Nanoscopic Insights of Amphiphilic Peptide against the Oligomer Assembly Process to Treat Huntington's Disease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis.Progress in molecular biology and translational science · 2020Review
- ATXN1 N-terminal region explains the binding differences of wild-type and expanded forms.BMC medical genomics · 2019Article
- New pathologic mechanisms in nucleotide repeat expansion disorders.Neurobiology of disease · 2019Review
- Polyglutamine Solution-State Structural Propensity Is Repeat Length Dependent.The journal of physical chemistry. B · 2019Article
- UV Resonance Raman Structural Characterization of an (In)soluble Polyglutamine Peptide.The journal of physical chemistry. B · 2019Article
- Temperature-induced collapse of a disordered peptide observed by three sampling methods in molecular dynamics simulations.The Journal of chemical physics · 2018Article
- Theory of Sequence Effects in Amyloid Aggregation.The journal of physical chemistry. B · 2018Article
- Tadpole-like Conformations of Huntingtin Exon 1 Are Characterized by Conformational Heterogeneity that Persists regardless of Polyglutamine Length.Journal of molecular biology · 2018Article
- Force field development and simulations of intrinsically disordered proteins.Current opinion in structural biology · 2018Review
5 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Abnormally expanded polyglutamine domains in proteins are associated with several neurodegenerative diseases, of which the best known is Huntington's. Expansion of the polyglutamine domain facilitates aggregation of the affected protein, and several studies directly link aggregation to neurotoxicity. The age of onset of disease is inversely correlated with the length of the polyglutamine domain; this correlation motivates an examination of the role of the length of the domain on aggregation. In this investigation, peptides containing 8 to 24 glutamines were synthesized, and their conformational and aggregation properties were examined. All peptides lacked secondary structure. Fluorescence resonance energy transfer studies revealed that the peptides became increasingly collapsed as the number of glutamine residues increased. The effective persistence length was estimated to decrease from approximately 11 to approximately 7 A as the number of glutamines increased from 8 to 24. A comparison of our data with theoretical results suggests that phosphate-buffered saline is a good solvent for Q8 and Q12, a theta solvent for Q16, and a poor solvent for Q20 and Q24. By dynamic light scattering, we observed that Q16, Q20, and Q24, but not Q8 or Q12, immediately formed soluble aggregates upon dilution into phosphate-buffered saline at 37 degrees C. Thus, Q16 stands at the transition point between good and poor solvent and between stable and aggregation-prone peptide. Examination of aggregates by transmission electron microscopy, along with kinetic assays for sedimentation, provided evidence indicating that soluble aggregates mature into sedimentable aggregates. Together, the data support a mechanism of aggregation in which monomer collapse is accompanied by formation of soluble oligomers; these soluble species lack regular secondary structure but appear morphologically similar to the sedimentable aggregates into which they eventually mature.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.