TY - JOUR
T1 - Inside Cover: Selective Inhibition of Aggregation and Toxicity of a Tau‐Derived Peptide using Its Glycosylated Analogues (Chem. Eur. J. 17/2016)
AU - Frenkel‐Pinter, Moran
AU - Abu‐Mokh, Amjaad
AU - Gazit, Ehud
AU - Rahimipour, Shai
AU - Segal, Daniel
PY - 2016
Y1 - 2016
N2 - 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.
AB - 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.
UR - https://harvester-2-eu.services.rm.elsevier.com/ws/6ced8d3b-d9ff-4f31-979a-0647230ba9f4/16867405-1b5e-47f3-8035-6f50dfa1d075/ws/files/58682874/Chemistry_A_European_Journal_2016_Frenkel_Pinter_Inside_Cover_Selective_Inhibition_of_Aggregation_and_Toxicity_of.pdf
UR - https://www.mendeley.com/catalogue/073d9c60-3580-3c9d-90f7-8cf54eafd6f9/
U2 - 10.1002/chem.201601078
DO - 10.1002/chem.201601078
M3 - Article
SN - 0947-6539
VL - 22
SP - 5798
EP - 5798
JO - Chemistry - A European Journal
JF - Chemistry - A European Journal
IS - 17
ER -