Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 79, Issue -, Pages 711-718Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2015.05.032
Keywords
Familial apolipoprotein A-I amyloidosis; Aggregation-prone peptide-analogues; Amyloid fibrils
Funding
- University of Athens
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Apolipoprotein A-I (apoA-I) is the major component of high density lipoproteins and plays a vital role in reverse cholesterol transport. Lipid-free apoA-I is the main constituent of amyloid deposits found in atherosclerotic plaques, an acquired type of amyloidosis, whereas its N-terminal fragments have been associated with a hereditary form, known as familial apoA-I amyloidosis. Here, we identified and verified four aggregation-prone segments of apoA-I with amyloidogenic properties, utilizing electron microscopy, X-ray fiber diffraction, ATR FT-IR spectroscopy and polarized light microscopy. These segments may act as conformational switches, possibly controlling the transition of the alpha-helical apoA-I content into the cross-beta architecture of amyloid fibrils. A structural model illuminating the structure of amyloid fibrils formed by the N-terminal fragments of apoA-I is proposed, indicating that two of the identified chameleon segments may play a vital part in the formation of amyloid fibrils in familial apoA-I amyloidosis. (C) 2015 Elsevier B.V. All rights reserved.
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