Sub-micellar phospholipid accelerates amyloid formation by apolipoprotein C-II
| Autor: | Lynne J. Lawrence, Geoffrey J. Howlett, Danny M. Hatters |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Protein Folding
Circular dichroism Time Factors Apolipoprotein C-II Biophysics Phospholipid Plasma protein binding Models Biological Biochemistry Micelle Protein Structure Secondary chemistry.chemical_compound Protein structure Nephelometry and Turbidimetry Structural Biology Genetics medicine Humans Apolipoproteins C Protein Structure Quaternary Dihexanoylphosphatidylcholine Molecular Biology Micelles Folding pathway Dose-Response Relationship Drug Chemistry Circular Dichroism Amyloidosis Cell Biology Atherosclerosis medicine.disease Molecular Weight Amyloid nucleation Phosphatidylcholines Analytical ultracentrifugation lipids (amino acids peptides and proteins) Protein folding Protein Binding |
| Zdroj: | FEBS Letters. 494:220-224 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(01)02355-9 |
| Popis: | Lipid-free human apolipoprotein C-II (apoC-II) forms amyloid fibrils with characteristic beta-structure. This conformation is distinct from the alpha-helical fold of lipid-bound apoC-II. We have investigated the effect of the short-chain phospholipid, dihexanoylphosphatidylcholine (DHPC) on amyloid formation by apoC-II. The alpha-helical content of apoC-II increases in the presence of micellar DHPC (16 mM) and amyloid formation is inhibited. However, at sub-micellar DHPC concentrations (below 8 mM) amyloid formation is accelerated 6 fold. These results suggest that individual phospholipid molecules in vivo may exert significant effects on amyloid folding pathways. |
| Databáze: | OpenAIRE |
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