Premium
Inside Cover: Selective Inhibition of Aggregation and Toxicity of a Tau‐Derived Peptide using Its Glycosylated Analogues (Chem. Eur. J. 17/2016)
Author(s) -
FrenkelPinter Moran,
Richman Michal,
Belostozky Anna,
AbuMokh Amjaad,
Gazit Ehud,
Rahimipour Shai,
Segal Daniel
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201601078
Subject(s) - glycan , chemistry , peptide , amyloid (mycology) , glycosylation , toxicity , biochemistry , stereochemistry , biophysics , biology , glycoprotein , organic chemistry , inorganic chemistry
Amyloid formation is attenuated by a single glycan unit. Using β‐O‐linked glycosylated variants of the Tau‐derived hexapeptide motif, VQIVYK, which served as a simplified amyloid model scaffold, it is demonstrated that amyloid formation and toxicity can be strongly attenuated by a glycan unit, depending on the nature of the glycan itself. Moreover, the glycosylated peptides inhibit aggregation of the corresponding non‐modified amyloid scaffold. More information can be found in the Full Paper by D. Segal, S. Rahimipour, E. Gazit et al. on page 5945 ff.