Identification of an amyloid fibril forming peptide comprising residues 46-59 of apolipoprotein A-I |
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Authors: | Wong Yuan Qi Binger Katrina J Howlett Geoffrey J Griffin Michael D W |
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Institution: | Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, Australia. |
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Abstract: | Apolipoprotein A-I (apoA-I) is deposited as amyloid within various major organs in hereditary apoA-I amyloidosis, and in arterial plaques associated with atherosclerosis. We have identified a tryptic fragment of apoA-I, apoA-I(46-59), that retains the ability to form amyloid-like fibrils with cross-β structure. ApoA-I(46-59) corresponds closely to a conformationally extended segment in the crystal structure of apoA-IΔ(185-243) and is located in the N-terminal region of apoA-I, which accumulates in hereditary apoA-I amyloidosis. Our results provide direct experimental evidence that this region of apoA-I is amyloidogenic and integral to initiation and propagation of amyloid formation by the protein. |
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