Premium
Embedding the Amyloid β‐Peptide Sequence in Green Fluorescent Protein Inhibits Aβ Oligomerization
Author(s) -
Takahashi Tsuyoshi,
Ohta Kenichi,
Mihara Hisakazu
Publication year - 2007
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200700108
Subject(s) - green fluorescent protein , peptide , sequence (biology) , fluorescence , embedding , barrel (horology) , construct (python library) , chemistry , amyloid (mycology) , biochemistry , peptide sequence , computational biology , biophysics , biology , gene , computer science , physics , artificial intelligence , inorganic chemistry , quantum mechanics , materials science , composite material , programming language
Against a green background . We have embedded the amyloid β‐peptide (Aβ) sequence into the green fluorescent protein (GFP) structure to generate a pseudo‐Aβ surface on the β‐barrel (see figure); this construct was highly active in inhibiting Aβ oligomerization. One GFP variant (P13H), which mimicked the parallel β sheets of Aβ, was found to bind Aβ with high affinity and inhibit Aβ oligomerization, even though the concentration of P13H was lower than that of Aβ.