ArticleACS omega2022
Distribution and Structure Analysis of Fibril-Forming Peptides Focusing on Concentration Dependency.
Article in ACS omega, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Hydrophobic and Electrostatic Sequence Patterning Directs Hierarchical Assembly of Phenylalanine-Rich Oligopeptides.The journal of physical chemistry letters · 2025Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We focus on the concentration dependency of fibril-forming peptides, which have the potential of aggregation by themselves. In this study, we performed replica-exchange molecular dynamics simulations of Lys-Phe-Phe-Glu (KFFE) fragments, which are known to form fibrils in experiments under different concentration environments. The analysis by static structure factors suggested that the density fluctuation of the KFFE fragments becomes large as the concentration increases. It was also found that the number of β-structures and oligomers also increases under a high concentration environment. Hence, a high concentration environment of fibril-forming peptides is likely to cause protein aggregation.
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Registered trials
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