In this section
@article{Lee:2018:10.3390/ijms19051357,
author = {Lee, C and Leanne, M and Liu, L-N and Madine, J and Davies, H},
doi = {10.3390/ijms19051357},
journal = {International Journal of Molecular Sciences},
title = {Insights into the origin of distinct medin fibril morphologies induced by incubation conditions and seeding.},
url = {http://dx.doi.org/10.3390/ijms19051357},
volume = {19},
year = {2018}
}
TY - JOUR
AB - Incubation conditions are an important factor to consider when studying protein aggregation in vitro. Here, we employed biophysical methods and atomic force microscopy to show that agitation dramatically alters the morphology of medin, an amyloid protein deposited in the aorta. Agitation reduces the lag time for fibrillation by ~18-fold, suggesting that the rate of fibril formation plays a key role in directing the protein packing arrangement within fibrils. Utilising preformed sonicated fibrils as seeds, we probed the role of seeding on medin fibrillation and revealed three distinct fibril morphologies, with biophysical modelling explaining the salient features of experimental observations. We showed that nucleation pathways to distinct fibril morphologies may be switched on and off depending on the properties of the seeding fibrils and growth conditions. These findings may impact on the development of amyloid-based biomaterials and enhance understanding of seeding as a pathological mechanism.
AU - Lee,C
AU - Leanne,M
AU - Liu,L-N
AU - Madine,J
AU - Davies,H
DO - 10.3390/ijms19051357
PY - 2018///
SN - 1661-6596
TI - Insights into the origin of distinct medin fibril morphologies induced by incubation conditions and seeding.
T2 - International Journal of Molecular Sciences
UR - http://dx.doi.org/10.3390/ijms19051357
UR - http://hdl.handle.net/10044/1/59767
VL - 19
ER -
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