Modulatory Effects of pH, Cu+2 and Sheet Breakers on Aggregation of Amyloid Peptides
| Autor: | Sarmistha Basak, Ajoy Basak, Xiaolei Hao, Kris Beking |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Circular dichroism
Amyloid Molecular Sequence Data chemistry.chemical_element Peptide Mass spectrometry Biochemistry Mass Spectrometry Protein Structure Secondary Ion Alzheimer Disease Structural Biology Humans Amino Acid Sequence Peptide sequence chemistry.chemical_classification Amyloid beta-Peptides Chemistry Circular Dichroism General Medicine Hydrogen-Ion Concentration Copper Peptide Fragments In vitro Crystallography Biophysics |
| Zdroj: | Protein & Peptide Letters. 12:197-202 |
| ISSN: | 0929-8665 |
| DOI: | 10.2174/0929866053005845 |
| Popis: | The study explores in vitro by circular dichroism and mass spectrometry the effects of pH, Cu+2 ions and sheet-breakers on the secondary structures and self-aggregation of beta-amyloid peptides [Abeta43, Abeta42 and Abeta40] of Alzheimer's disease. Within pH 5.4-7.3, more sheet structures and aggregates containing up to 11 peptide units were observed. Cu+2 ions led to oxidative degradation or aggregation depending on its concentration and time of incubation. beta-sheet breakers can reverse the self-aggregation process, suggesting their potential therapeutic use. |
| Databáze: | OpenAIRE |
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