Amyloid formation of native folded protein induced by peptide-based graft copolymer.
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-beta form (inter-strand spacing: 4.65 A and inter-sheet spacing: 10.65 A) 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.
Koga
Tomoyuki
T
Nanoarchitectonics Research Center, National Institute of Advanced Industrial Science and Technology and CREST (Japan Science and Technology Corporation), Tsukuba Central 5, 1-1-1, Higashi, Tsukuba Ibaraki 305-8565, Japan.
Taguchi
Kazuhiro
K
Kogiso
Masaki
M
Kobuke
Yoshiaki
Y
Kinoshita
Takatoshi
T
Higuchi
Masahiro
M
D000682:Amyloid / Q000378:metabolism / Q000648:ultrastructure; D000818:Animals; D002942:Circular Dichroism; D003224:Congo Red / Q000737:chemistry / Q000378:metabolism; D021621:Imaging, Three-Dimensional; D018625:Microscopy, Atomic Force; D009211:Myoglobin / Q000737:chemistry / Q000187:drug effects / Q000648:ultrastructure*; D010455:Peptides; D011073:Polyamines / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D011108:Polymers / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D014961:X-Ray Diffraction
D000682:Amyloid; D009211:Myoglobin; D010455:Peptides; D011073:Polyamines; D011108:Polymers; D011506:Proteins; C468911:poly(gamma-methylglutamate)-grafted polyallylamine; D003224:Congo Red