TY - JOUR TI - Chameleon ‘aggregation-prone’ segments of apoA-I: A model of amyloid fibrils formed in apoA-I amyloidosis AU - Louros, N.N., AU - Tsiolaki, P.L., AU - Griffin, M.D., AU - Howlett, G.J., AU - Hamodrakas, S.J., AU - Iconomidou, V.A. JO - INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES PY - 2015 VL - 79 TODO - 1 SP - 711-719 PB - Elsevier SN - 0141-8130 TODO - null TODO - Familial apolipoprotein A-I amyloidosis, “Aggregation-prone” peptide-analogues, Amyloid fibrils TODO - 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 -helical apoA-I content into the “cross-” 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. ER -