TY - JOUR
AU - Galzitskaya, Oxana V.
AB - AbstractThe aim of this study was to investigate the process of amyloidogenesis of amyloid-β(Aβ)42 peptide, by means of fluorescence spectroscopy, electron microscopy,X-ray diffraction, and mass spectrometry. It has been repeatedly reported in theliterature that the process of fibril formation by Aβ 42 peptide dependsconsiderably not only upon the specific conditions (ionic conditions, pH, temperature,mixing, etc.), as well as the manufacturing route (synthetic or recombinant), but also onthe methods of synthesis and purification. We have, for the first time, systematicallyanalyzed samples of Aβ 42 peptide supplied by five different companies(Anaspec, Invitrogen, Enzo, Sigma-Aldrich, and SynthAssist) and obtained evidence ofsignificant variability, including lot to lot variations. All studied samples formedamyloid-like fibrils at pH3-6, and the fibrils contained cross-β structures. Samples fromAnaspec, Invitrogen, and Enzo formed one particular type of amyloid-like fibrils, whilethe samples from Sigma-Aldrich and SynthAssist formed another distinct type of fibrils.The observed polymorphism emphasizes the capacity of the Aβ 42 peptide to actas a prion agent with varying structural characteristics. The presented data have allowedus to propose a possible mechanism of formation of amyloid-like fibrils.
TI - Studies of Polymorphism of Amyloid-β 42 Peptide from Different          Suppliers
JO - Journal of Alzheimer's Disease
DO - 10.3233/jad-150147
DA - 2015-08-03
UR - https://www.deepdyve.com/lp/ios-press/studies-of-polymorphism-of-amyloid-42-peptide-from-different-suppliers-3KigejP7zN
SP - 583
EP - 593
VL - 47
IS - 3
DP - DeepDyve
ER -