Publication | Closed Access
Characterizing Early Aggregates Formed by an Amyloidogenic Peptide by Mass Spectrometry
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Citations
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References
2010
Year
Biological Mass SpectrometryMolecular BiologyNeurochemical BiomarkersPeptide ScienceAnalytical UltracentrifugationEarly AggregatesAlzheimer's DiseaseProtein FoldingBioanalysisProtein MisfoldingProteomicsAmyloidogenic EndecapeptideBiophysicsAmyloidogenic PeptideBiochemistryBiomolecular ScienceNatural SciencesMass SpectrometryProtein Mass SpectrometryPeptide TherapeuticEarly Aggregation StatesMedicine
What floats in the soup? Time-course and ion-mobility nano-electrospray ionization (nESI) mass spectrometry probes the early aggregation states of an amyloidogenic endecapeptide derived from amino acid residues 105–115 of the human plasma protein transthyretin. A wide range of densely packed prefibrillar oligomers 1≤n≤13 are observed in dynamic populations over 8 h. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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