TY - JOUR
T1 - Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core
AU - Bera, Santu
AU - Arad, Elad
AU - Schnaider, Lee
AU - Shaham-Niv, Shira
AU - Castelletto, Valeria
AU - Peretz, Yossef
AU - Zaguri, Dor
AU - Jelinek, Raz
AU - Gazit, Ehud
AU - Hamley, Ian W.
N1 - Publisher Copyright:
© 2019 The Royal Society of Chemistry.
PY - 2019
Y1 - 2019
N2 - The amino acid sequence plays an essential role in amyloid formation. Here, using the central core recognition module of the Aβ peptide and its reverse sequence, we show that although both peptides assemble into β-sheets, their morphologies, kinetics and cell toxicities display marked differences. In addition, the native peptide, but not the reverse one, shows notable affinity towards bilayer lipid model membranes that modulates the aggregation pathways to stabilize the oligomeric intermediate states and function as the toxic agent responsible for neuronal dysfunction.
AB - The amino acid sequence plays an essential role in amyloid formation. Here, using the central core recognition module of the Aβ peptide and its reverse sequence, we show that although both peptides assemble into β-sheets, their morphologies, kinetics and cell toxicities display marked differences. In addition, the native peptide, but not the reverse one, shows notable affinity towards bilayer lipid model membranes that modulates the aggregation pathways to stabilize the oligomeric intermediate states and function as the toxic agent responsible for neuronal dysfunction.
UR - http://www.scopus.com/inward/record.url?scp=85069479870&partnerID=8YFLogxK
U2 - 10.1039/c9cc03654g
DO - 10.1039/c9cc03654g
M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???
AN - SCOPUS:85069479870
VL - 55
SP - 8595
EP - 8598
JO - Chemical Communications
JF - Chemical Communications
SN - 1359-7345
IS - 59
ER -