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Heterogeneous Assembly of Complementary Peptide Pairs into Amyloid Fibrils with α–β Structural Transition
Author(s) -
Takahashi Yuta,
Ueno Akihiko,
Mihara Hisakazu
Publication year - 2001
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20010105)2:1<75::aid-cbic75>3.0.co;2-u
Subject(s) - peptide , fibril , amyloid fibril , chemistry , biophysics , self assembly , amyloid (mycology) , helix (gastropod) , transition (genetics) , lysine , beta sheet , crystallography , amyloid β , amino acid , biochemistry , biology , organic chemistry , medicine , inorganic chemistry , disease , pathology , gene , ecology , snail
The self‐initiated structural transition from an initially formed α‐helix structure to a β‐sheet structure is the prerequisite for the spontaneous assembly of complementary peptide pairs into amyloid fibrils. The heterogeneous assembly is accomplished by favorable electrostatic interactions between pairs of designed peptide species that contain positively charged lysine (K) residues and negatively charged glutamate (E) residues (see picture).