Evidence map›Paper›PMID 36120541›Full record

ArticleFrontiers in molecular biosciences2022

Exploring the misfolding and self-assembly mechanism of TTR (105-115) peptides by all-atom molecular dynamics simulation.

Yuqi Zhang, Yanyan Zhu, Haiyan Yue, Qingjie Zhao, Huiyu Li

Abstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Yuqi ZhangCollege of Mathematics and Physics, Shanghai University of Electric Power, Shanghai, China.
Yanyan ZhuCollege of Mathematics and Physics, Shanghai University of Electric Power, Shanghai, China.
Haiyan YueNaval Medical Center of PLA, Department of Digestive Diseases, Naval Medical University, Shanghai, China.
Qingjie ZhaoInnovation Research Institute of Traditional Chinese Medicine, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Huiyu LiCollege of Mathematics and Physics, Shanghai University of Electric Power, Shanghai, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pathological aggregation of essentially dissociative Transthyretin (TTR) monomers protein, driven by misfolded and self-interaction, is connected with Amyloid Transthyretin amyloidosis (ATTR) disease. The TTR monomers protein contains several fragments that tend to self-aggregate, such as residue 105-115 sequence [TTR (105-115)]. However, the misfolding and aggregation mechanisms of TTR are still unknown. In this study, we explored the misfolding and self-assembly of TTR (105-115) peptides by all-atom molecular dynamics simulation. Our results indicated that the conformation of the two-peptides appears unstable. In the tetramerization and hexamerization simulations, the results are reversed. When the number of peptides increases, the probability and the length of

Indexed as

ATTRhydrophobic interactionmolecular dynamics simulationpeptide aggregationTTR(105–115)β-Barrel

Identifiers

PMID36120541
PMCPMC9473747

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.