Modulating Aβ 33–42  Peptide Assembly by Graphene Oxide | Zendy

Li Qiang | Zendy; Liu Lei | Zendy; Zhang Shuai | Zendy; Xu Meng | Zendy; Wang Xueqin | Zendy; Wang Chen | Zendy; Besenbacher Flemming | Zendy; Dong Mingdong | Zendy

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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.

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