TY - JOUR
T1 - A bifunctional non-natural tetrapeptide modulates amyloid-beta peptide aggregation in the presence of Cu(II)
AU - Márquez, Maripaz
AU - Blancas-Mejía, Luis M.
AU - Campos, Adriana
AU - Rojas, Luis
AU - Castañeda-Hernández, Gilberto
AU - Quintanar, Liliana
N1 - Publisher Copyright:
© The Royal Society of Chemistry 2014.
PY - 2014/12/1
Y1 - 2014/12/1
N2 - Amyloid-beta peptide (Aβ) aggregation is one of the hallmarks of Alzheimer's disease (AD), and metal ions such as Cu(ii) have been proposed to play a role in amyloid formation and the onset of this progressive neurodegenerative disorder. This study reports the design and characterization of a novel bifunctional non-natural tetrapeptide, Met-Asp-d-Trp-Aib, that is capable of binding copper, competing with Aβ for Cu(ii), and modulating Aβ aggregation. The study of this tetrapeptide provides further insights into the role of Cu(ii) in the Aβ aggregation pathway, and into the design of compounds with therapeutic potential for Alzheimer's disease.
AB - Amyloid-beta peptide (Aβ) aggregation is one of the hallmarks of Alzheimer's disease (AD), and metal ions such as Cu(ii) have been proposed to play a role in amyloid formation and the onset of this progressive neurodegenerative disorder. This study reports the design and characterization of a novel bifunctional non-natural tetrapeptide, Met-Asp-d-Trp-Aib, that is capable of binding copper, competing with Aβ for Cu(ii), and modulating Aβ aggregation. The study of this tetrapeptide provides further insights into the role of Cu(ii) in the Aβ aggregation pathway, and into the design of compounds with therapeutic potential for Alzheimer's disease.
UR - http://www.scopus.com/inward/record.url?scp=84911482662&partnerID=8YFLogxK
U2 - 10.1039/c4mt00257a
DO - 10.1039/c4mt00257a
M3 - Artículo
SN - 1756-5901
VL - 6
SP - 2189
EP - 2192
JO - Metallomics
JF - Metallomics
IS - 12
ER -