| VÁCHA, Robert, S. LINSE and M. LUND. Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides. Journal of the American Chemical Society. Washington, D.C.: American Chemical Society, 2014, vol. 136, No 33, p. 11776-11782. ISSN 0002-7863. Available from: https://dx.doi.org/10.1021/ja505502e. |
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@article{1197997,
author = {Vácha, Robert and Linse, S. and Lund, M.},
article_location = {Washington, D.C.},
article_number = {33},
doi = {http://dx.doi.org/10.1021/ja505502e},
keywords = {BETA PROTEIN FIBRILLATION; ALPHA-SYNUCLEIN; POLYMERIC NANOPARTICLES; MEMBRANE INTERACTIONS; LIPID-BILAYERS; DRUG-DELIVERY; PHASE; NUCLEATION; INHIBITION; INTERFACES},
language = {eng},
issn = {0002-7863},
journal = {Journal of the American Chemical Society},
title = {Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides},
url = {http://pubs.acs.org/doi/abs/10.1021/ja505502e},
volume = {136},
year = {2014}
}
TY - JOUR
ID - 1197997
AU - Vácha, Robert - Linse, S. - Lund, M.
PY - 2014
TI - Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides
JF - Journal of the American Chemical Society
VL - 136
IS - 33
SP - 11776-11782
EP - 11776-11782
PB - American Chemical Society
SN - 00027863
KW - BETA PROTEIN FIBRILLATION
KW - ALPHA-SYNUCLEIN
KW - POLYMERIC NANOPARTICLES
KW - MEMBRANE INTERACTIONS
KW - LIPID-BILAYERS
KW - DRUG-DELIVERY
KW - PHASE
KW - NUCLEATION
KW - INHIBITION
KW - INTERFACES
UR - http://pubs.acs.org/doi/abs/10.1021/ja505502e
L2 - http://pubs.acs.org/doi/abs/10.1021/ja505502e
N2 - The presence of surfaces influences the fibril formation kinetics of peptides and proteins. We present a systematic study of the aggregation kinetics of amyloidogenic peptides caused by different surfaces using molecular simulations of model peptides and thioflavin T fluorescence experiments. Increasing the monomer surface attraction affects the nucleation and growth of small oligomers in a nonlinear manner: Weakly attractive surfaces lead to retardation; strongly attractive surfaces lead to acceleration. Further, the same type of surface either accelerates or retards growth, depending on the bulk propensity of the peptide to form fibrils: An attractive surface retards fibril formation of peptides with a high tendency for fibril formation, while the same surface accelerates fibril formation of peptides with a low propensity for fibril formation. The surface effect is thus determined by the relative association propensity of peptides for the surface compared to bulk and by the surface area to protein concentration ratio. This rationalization is in agreement with the measured fibrillar growth of a-synuclein from Parkinson and amyloid beta peptide from Alzheimer disease in the presence of surface area introduced in a controlled way in the form of nanoparticles. These findings offer molecular insight into amyloid formation kinetics in complex environments and may be used to tune fibrillation properties in diverse systems.
ER -
VÁCHA, Robert, S. LINSE and M. LUND. Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides. \textit{Journal of the American Chemical Society}. Washington, D.C.: American Chemical Society, 2014, vol.~136, No~33, p.~11776-11782. ISSN~0002-7863. Available from: https://dx.doi.org/10.1021/ja505502e.
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