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Effects of oxidation, pH and lipids on amyloidogenic peptide structure: implications for fibril formation?
- Source :
-
European Biophysics Journal . Nov2008, Vol. 38 Issue 1, p99-110. 12p. 2 Diagrams, 5 Graphs. - Publication Year :
- 2008
-
Abstract
- We have performed experimental and computational studies to investigate the influences of phospholipids, methionine oxidation and acidic pH on amyloid fibril formation by a peptide derived from human apolipoprotein C-II (apoC-II), a known component of proteinaceous atherosclerotic plaques. Fibril growth monitored by thioflavin T fluorescence revealed inhibition under lipid-rich and oxidising conditions. We subsequently performed fully-solvated atomistic molecular dynamics (MD) simulations of the peptide monomer to study its conformations under both fibril favouring (neutral and low pH) and inhibiting (lipid-rich and oxidising) conditions. Examination of the chain topology, backbone hydrogen-bonding patterns and aromatic sidechain orientations of the peptide under different conditions reveals that, while the peptide adopts similar structures under the fibril-favouring conditions, significantly different structures are obtained under fibril-disruptive conditions. Based on our results, we advance hypotheses for the roles of peptide conformation on aggregation and fibrillisation propensities. [ABSTRACT FROM AUTHOR]
- Subjects :
- *PHOSPHOLIPIDS
*METHIONINE
*OXIDATION
*PEPTIDES
*HYDROGEN bonding
Subjects
Details
- Language :
- English
- ISSN :
- 01757571
- Volume :
- 38
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- European Biophysics Journal
- Publication Type :
- Academic Journal
- Accession number :
- 34982814
- Full Text :
- https://doi.org/10.1007/s00249-008-0363-3