Solubility Parameters of Amino Acids on Liquid–Liquid Phase Separation and Aggregation of Proteins
Frontiers in Cell and Developmental Biology, ISSN: 2296-634X, Vol: 9, Page: 691052
2021
- 10Citations
- 43Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations10
- Citation Indexes10
- 10
- Captures43
- Readers43
- 43
Article Description
The solution properties of amino acids determine the folding, aggregation, and liquid–liquid phase separation (LLPS) behaviors of proteins. Various indices of amino acids, such as solubility, hydropathy, and conformational parameter, describe the behaviors of protein folding and solubility both in vitro and in vivo. However, understanding the propensity of LLPS and aggregation is difficult due to the multiple interactions among different amino acids. Here, the solubilities of aromatic amino acids (SAs) were investigated in solution containing 20 types of amino acids as amino acid solvents. The parameters of SAs in amino acid solvents (PSASs) were varied and dependent on the type of the solvent. Specifically, Tyr and Trp had the highest positive values while Glu and Asp had the lowest. The PSAS values represent soluble and insoluble interactions, which collectively are the driving force underlying the formation of droplets and aggregates. Interestingly, the PSAS of a soluble solvent reflected the affinity between amino acids and aromatic rings, while that of an insoluble solvent reflected the affinity between amino acids and water. These findings suggest that the PSAS can distinguish amino acids that contribute to droplet and aggregate formation, and provide a deeper understanding of LLPS and aggregation of proteins.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85109047920&origin=inward; http://dx.doi.org/10.3389/fcell.2021.691052; http://www.ncbi.nlm.nih.gov/pubmed/34222258; https://www.frontiersin.org/articles/10.3389/fcell.2021.691052/full; https://dx.doi.org/10.3389/fcell.2021.691052; https://www.frontiersin.org/journals/cell-and-developmental-biology/articles/10.3389/fcell.2021.691052/full
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