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Novel conformation‐selective monoclonal antibodies against apoA‐I amyloid fibrils
Author(s) -
Ohgita Takashi,
Furutani Yuki,
Nakano Miyu,
Hattori Megumi,
Suzuki Ayane,
Nakagawa Miho,
Naniwa Sera,
Morita Izumi,
Oyama Hiroyuki,
Nishitsuji Kazuchika,
Kobayashi Norihiro,
Saito Hiroyuki
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15487
Subject(s) - fibril , chemistry , monoclonal antibody , amyloidosis , amyloid (mycology) , antibody , apolipoprotein b , biochemistry , microbiology and biotechnology , biology , immunology , cholesterol , medicine , pathology , inorganic chemistry
The N‐terminal 1–83 fragment of human apolipoprotein A‐I (apoA‐I) carrying G26R mutation forms amyloid fibrils that potentially cause hereditary amyloidosis. We generated monoclonal antibodies that specifically bind to amyloid fibrils composed of not only apoA‐I fragment but also α‐synuclein. In silico modeling suggests that the antibodies might recognize the characteristic quaternary structures, constructed due to parallel stacking of VYV (in apoA‐I fragment) or LYV (in α‐synuclein) motifs.