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Inhibition of Amyloid Fibril Formation by Peptide Analogues Modified with α‐Aminoisobutyric Acid
Author(s) -
Gilead Sharon,
Gazit Ehud
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200353565
Subject(s) - aminoisobutyric acid , amyloid fibril , fibril , peptide , amino acid , chemistry , amyloid (mycology) , biophysics , biochemistry , amyloid β , biology , medicine , inorganic chemistry , disease , pathology
Breaking up is not hard to do with an α‐aminoisobutyric (Aib) acid β‐breaker, which has a remarkably restricted conformation. A novel approach to the inhibition of amyloid formation was developed that uses peptides modified with Aib (see figure). The similarity of Aib to hydrophobic amino acids, often found in amyloidogenic sequences, allows its integration into recognition motifs.