Stochastic master equation for early protein aggregation in the transthyretin amyloid disease
Abstract It is significant to understand the earliest molecular events occurring in the nucleation of the amyloid aggregation cascade for the prevention of amyloid related diseases such as transthyretin amyloid disease. We develop chemical master equation for the aggregation of monomers into oligome...
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Nature Portfolio
2020
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oai:doaj.org-article:fdada9857a73460eb14fb984d9f8549b2021-12-02T17:55:13ZStochastic master equation for early protein aggregation in the transthyretin amyloid disease10.1038/s41598-020-69319-x2045-2322https://doaj.org/article/fdada9857a73460eb14fb984d9f8549b2020-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-69319-xhttps://doaj.org/toc/2045-2322Abstract It is significant to understand the earliest molecular events occurring in the nucleation of the amyloid aggregation cascade for the prevention of amyloid related diseases such as transthyretin amyloid disease. We develop chemical master equation for the aggregation of monomers into oligomers using reaction rate law in chemical kinetics. For this stochastic model, lognormal moment closure method is applied to track the evolution of relevant statistical moments and its high accuracy is confirmed by the results obtained from Gillespie’s stochastic simulation algorithm. Our results show that the formation of oligomers is highly dependent on the number of monomers. Furthermore, the misfolding rate also has an important impact on the process of oligomers formation. The quantitative investigation should be helpful for shedding more light on the mechanism of amyloid fibril nucleation.Ruo-Nan LiuYan-Mei KangNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-9 (2020) |
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Medicine R Science Q Ruo-Nan Liu Yan-Mei Kang Stochastic master equation for early protein aggregation in the transthyretin amyloid disease |
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Abstract It is significant to understand the earliest molecular events occurring in the nucleation of the amyloid aggregation cascade for the prevention of amyloid related diseases such as transthyretin amyloid disease. We develop chemical master equation for the aggregation of monomers into oligomers using reaction rate law in chemical kinetics. For this stochastic model, lognormal moment closure method is applied to track the evolution of relevant statistical moments and its high accuracy is confirmed by the results obtained from Gillespie’s stochastic simulation algorithm. Our results show that the formation of oligomers is highly dependent on the number of monomers. Furthermore, the misfolding rate also has an important impact on the process of oligomers formation. The quantitative investigation should be helpful for shedding more light on the mechanism of amyloid fibril nucleation. |
format |
article |
author |
Ruo-Nan Liu Yan-Mei Kang |
author_facet |
Ruo-Nan Liu Yan-Mei Kang |
author_sort |
Ruo-Nan Liu |
title |
Stochastic master equation for early protein aggregation in the transthyretin amyloid disease |
title_short |
Stochastic master equation for early protein aggregation in the transthyretin amyloid disease |
title_full |
Stochastic master equation for early protein aggregation in the transthyretin amyloid disease |
title_fullStr |
Stochastic master equation for early protein aggregation in the transthyretin amyloid disease |
title_full_unstemmed |
Stochastic master equation for early protein aggregation in the transthyretin amyloid disease |
title_sort |
stochastic master equation for early protein aggregation in the transthyretin amyloid disease |
publisher |
Nature Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/fdada9857a73460eb14fb984d9f8549b |
work_keys_str_mv |
AT ruonanliu stochasticmasterequationforearlyproteinaggregationinthetransthyretinamyloiddisease AT yanmeikang stochasticmasterequationforearlyproteinaggregationinthetransthyretinamyloiddisease |
_version_ |
1718379147704664064 |