ArticleThe journal of physical chemistry letters2023
Fatty Acids Reverse the Supramolecular Chirality of Insulin Fibrils.
Article in The journal of physical chemistry letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed.
- Single Amino Acid-Based Control of Fibril Supramolecular Chirality.The journal of physical chemistry letters · 2026Article
- Elucidating the mechanisms of α-Synuclein-lipid interactions using site-directed mutagenesis.Neurobiology of disease · 2024Article
- Tubulin-binding region alters tau-lipid interactions and changes toxicity of tau fibrils formed in the presence of phosphatidylserine lipids.Protein science : a publication of the Protein Society · 2024Article
- The influence of zwitterionic and anionic phospholipids on protein aggregation.Biophysical chemistry · 2024Review
- Secondary structure and toxicity of lysozyme fibrils are determined by the length and unsaturation of phosphatidic acid.Proteins · 2024Article
- Long-Chain Polyunsaturated Fatty Acids Accelerate the Rate of Insulin Aggregation and Enhance Toxicity of Insulin Aggregates.ACS chemical neuroscience · 2024Article
- Elucidating the Role of Lipids in the Aggregation of Amyloidogenic Proteins.Accounts of chemical research · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Long-chain unsaturated and polyunsaturated fatty acids (LCUFAs and LCPUFAs, respectively) are the essential components of phospholipids and sphingolipids, major building blocks of plasma and organelle membranes. These molecules are also involved in cell signaling and energy metabolism. Hence, both LCUFAs and LCPUFAs are broadly used as food supplements. However, the role of these fatty acids (FAs) in the self-assembly of misfolded proteins remains unclear. In this study, we investigated the effect of LCUFAs and LCPUFAs, as well as their saturated analogue, on insulin aggregation. Using vibrational circular dichroism, we found that all analyzed FAs reversed the supramolecular chirality of insulin fibrils. Molecular dynamics simulations showed that strong hydrophobic interactions were formed between the long aliphatic tails of FAs and hydrophobic amino acid residues of insulin. We infer that such insulin:FA complexes had different self-assembly mechanisms compared to that of insulin alone, which resulted in the observed reversal of the supramolecular chirality of the amyloid fibrils.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.