ArticleThe journal of physical chemistry letters2024
Amino Acids and Their Biological Derivatives Modulate Protein-Protein Interactions in an Additive Way.
Article in The journal of physical chemistry letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- The influence of proline on surface interactions in aqueous solutions.Biophysical journal · 2025Article
- Amino acids bind to phase-separating proteins and modulate biomolecular condensate stability and dynamics.Nature communications · 2025Article
- Article
- Amino acids modulate liquid-liquid phase separation in vitro and in vivo by regulating protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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2 authors.
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Abstract
Protein-protein interactions (PPIs) differ when measured in test tubes and cells due to the complexity of the intracellular environment. Free amino acids (AAs) and their derivatives constitute a significant fraction of the intracellular volume and mass. Recently, we have found that AAs have a generic property of rendering protein dispersions more stable by reducing the net attractive part of PPIs. Here, we study the effects on PPIs of different AA derivatives, AA mixtures, and short peptides. We find that all the tested AA derivatives modulate PPIs in solution as effectively as AAs. Furthermore, we show that the modulation effect is additive when AAs form mixtures or are bound into short peptides. Therefore, this study demonstrates the additive effects of a class of small molecules (i.e., AAs and their biological derivatives) on PPIs and provides insights into rationally designing biocompatible molecules for stabilizing protein interactions and consequently tuning protein functions.
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