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Modulating Aβ 33–42 Peptide Assembly by Graphene Oxide
Author(s) -
Li Qiang,
Liu Lei,
Zhang Shuai,
Xu Meng,
Wang Xueqin,
Wang Chen,
Besenbacher Flemming,
Dong Mingdong
Publication year - 2014
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201402022
Subject(s) - graphene , oxide , peptide , amyloid fibril , nanotechnology , amyloid (mycology) , materials science , fibril , amyloidosis , atomic force microscopy , biophysics , monomer , chemistry , amyloid β , biochemistry , inorganic chemistry , pathology , medicine , polymer , biology , composite material , disease , metallurgy
Graphene oxide (GO) is utilized as the modulator to tune the formation and development of amyloid fibrils (Aβ 33–42 ). Atomic force microscopy temporal evolution measurements reveal that the initial binding between the peptide monomer and the large available surface of the GO sheets can redirect the assembly pathway of amyloid beta. The results support the possibility to develop graphene‐based materials to inhibit amyloidosis.