@misc{10481/80470,
year = {2021},
month = {4},
url = {https://hdl.handle.net/10481/80470},
abstract = {We present the optimization of experimental
conditions to yield long, rigid apoferritin protein amyloid fibrils,
as well as the corresponding fibrillation pathway. Fibril growth
kinetics was followed using atomic force microscopy (AFM),
transmission electron microscopy (TEM), dynamic light scattering
(DLS), circular dichroism (CD), fourier-transform infrared
spectroscopy (FTIR), and sodium dodecyl sulfate polyacrylamide
gel electrophoresis (SDS-PAGE). Among the morphologies
identified, we show that the conditions result in small aggregates,
as well as medium and long fibrils. Extended incubation times led
to progressive unfolding and hydrolysis of the proteins into very short peptide fragments. AFM, SDS-PAGE, and CD support a
universal common fibrillation mechanism in which hydrolyzed fragments play the central role. These collective results provide
convincing evidence that protein unfolding and complete hydrolysis of the proteins into very short peptide sequences are essential
for the formation of the final apoferritin amyloid-like fibrils.},
organization = {Junta de Andalucia	P11-FQM-8136
P18-RT-1373},
organization = {Ministry of Science and Innovation, Spain (MICINN)},
organization = {Instituto de Salud Carlos III},
organization = {Spanish Government	PID2019-111461GB-I00},
organization = {Boehringer Ingelheim},
publisher = {American Chemical Society},
title = {Understanding the Formation of Apoferritin Amyloid Fibrils},
doi = {10.1021/acs.biomac.1c00176},
author = {Jurado Palomares, Rocío and Gálvez Rodríguez, Natividad},
}