ArticlePhysical chemistry chemical physics : PCCP2021
Studying the mechanism of phase separation in aqueous solutions of globular proteins
Article in Physical chemistry chemical physics : PCCP, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Surface Charge Can Modulate Phase Separation of Multidomain Proteins.Journal of the American Chemical Society · 2024Article
- Protein Association in Solution: Statistical Mechanical Modeling.Biomolecules · 2023Review
- The mechanism of self-association of humanJournal of molecular liquids · 2023Article
- The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions.International journal of molecular sciences · 2023Article
- Mechanistic differences in the effects of sucrose and sucralose on the phase stability of lysozyme solutions.Journal of molecular liquids · 2021Article
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Authors and funding
4 authors.
Funding
Abstract
Proteins are the most abundant biomacromolecules in living cells, where they perform vital roles in virtually every biological process. To maintain their function, proteins need to remain in a stable (native) state. Inter- and intramolecular interactions in aqueous protein solutions govern the fate of proteins, as they can provoke their unfolding or association into aggregates. The initial steps of protein aggregation are difficult to capture experimentally, therefore we used molecular dynamics simulations in this study. We investigated the initial phase of aggregation of two different lysozymes, hen egg-white (HEWL) and T4 WT* lysozyme and also human lens γ-D crystallin by using atomistic simulations. We monitored the phase stability of their aqueous solutions by calculating time-dependent density fluctuations. We found that all proteins remained in their compact form despite aggregation. With an extensive analysis of intermolecular residue-residue interactions we discovered that arginine is of paramount importance in the initial stage of aggregation of HEWL and γ-D crystallin, meanwhile lysine was found to be the most involved amino acid in forming initial contacts between T4 WT* molecules.
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Registered trials
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