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Amyloid formation of native folded protein induced by peptide‐based graft copolymer
Author(s) -
Koga Tomoyuki,
Taguchi Kazuhiro,
Kogiso Masaki,
Kobuke Yoshiaki,
Kinoshita Takatoshi,
Higuchi Masahiro
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03438-5
Subject(s) - myoglobin , fibril , peptide , globular protein , congo red , amyloid fibril , amyloid (mycology) , chemistry , biophysics , amyloidosis , beta sheet , native state , biochemistry , amyloid β , biology , organic chemistry , medicine , inorganic chemistry , disease , adsorption , pathology
We report here that a native folded holo ‐myoglobin, when incubated with a synthetic amyloidogenic peptide in aqueous solutions, forms fibrils. These fibrils took a cross‐β form (inter‐strand spacing: 4.65 Å and inter‐sheet spacing: 10.65 Å) and bound the amyloidophilic dye Congo red as did the authentic amyloid fibrils. In contrast such fibril formation of myoglobin did not occur in the absence of the peptide. These results suggest the possibility that inter‐molecular interaction of native protein with the amyloidogenic peptide trigger the amyloid formation even for the non‐pathogenic native protein like myoglobin, which itself exists as a globular form, under certain conditions.