The extreme N-terminal region of human apolipoprotein A-I has a strong propensity to form amyloid fibrils |
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Authors: | Emi Adachi Asako Kosaka Kohei Tsuji Chiharu Mizuguchi Hiroyuki Kawashima Akira Shigenaga Kohjiro Nagao Kenichi Akaji Akira Otaka Hiroyuki Saito |
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Affiliation: | 1. Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima, 1-78-1 Shomachi, Tokushima 770-8505, Japan;2. Department of Medicinal Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, Kyoto 607-8412, Japan |
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Abstract: | The N-terminal 1–83 residues of apolipoprotein A-I (apoA-I) have a strong propensity to form amyloid fibrils, in which the 46–59 segment was reported to aggregate to form amyloid-like fibrils. In this study, we demonstrated that a fragment peptide comprising the extreme N-terminal 1–43 residues strongly forms amyloid fibrils with a transition to β-sheet-rich structure, and that the G26R point mutation enhances the fibril formation of this segment. Our results suggest that in addition to the 46–59 segment, the extreme N-terminal region plays a crucial role in the development of amyloid fibrils by the N-terminal fragment of amyloidogenic apoA-I variants. |
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Keywords: | Apolipoprotein A-I Amyloid fibril Peptide Point mutation |
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