ArticleScientific reports2021
Characterization of design grammar of peptides for regulating liquid droplets and aggregates of FUS.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Biomolecular coacervation-mediated materials: Phase states, phase transitions, and biomedical applications.Bioactive materials · 2027Review
- Coacervate-pore complexes for selective molecular transport and dynamic reconfiguration.Nature communications · 2024Article
- Leveraging a large language model to predict protein phase transition: A physical, multiscale, and interpretable approach.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- An aberrant fused in sarcoma liquid droplet of amyotrophic lateral sclerosis pathological variant, R495X, accelerates liquid-solid phase transition.Scientific reports · 2024Article
- Rational design of phase separating peptides based on phase separating protein sequence of p53.Scientific reports · 2023Article
- Rational peptide design for regulating liquid-liquid phase separation on the basis of residue-residue contact energy.Scientific reports · 2022Article
- Structure-dependent recruitment and diffusion of guest proteins in liquid droplets of FUS.Scientific reports · 2022Article
- Molecular principles of recruitment and dynamics of guest proteins in liquid droplets.Scientific reports · 2021Article
- Single-Molecule Microscopy Meets Molecular Dynamics Simulations for Characterizing the Molecular Action of Proteins on DNA and in Liquid Condensates.Frontiers in molecular biosciences · 2021Review
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Authors and funding
11 authors.
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Abstract
Liquid droplets of aggregation-prone proteins, which become hydrogels or form amyloid fibrils, are a potential target for drug discovery. In this study, we proposed an experiment-guided protocol for characterizing the design grammar of peptides that can regulate droplet formation and aggregation. The protocol essentially involves investigation of 19 amino acid additives and polymerization of the identified amino acids. As a proof of concept, we applied this protocol to fused in sarcoma (FUS). First, we evaluated 19 amino acid additives for an FUS solution and identified Arg and Tyr as suppressors of droplet formation. Molecular dynamics simulations suggested that the Arg additive interacts with specific residues of FUS, thereby inhibiting the cation-π and electrostatic interactions between the FUS molecules. Second, we observed that Arg polymers promote FUS droplet formation, unlike Arg monomers, by bridging the FUS molecules. Third, we found that the Arg additive suppressed solid aggregate formation of FUS, while Arg polymer enhanced it. Finally, we observed that amyloid-forming peptides induced the conversion of FUS droplets to solid aggregates of FUS. The developed protocol could be used for the primary design of peptides controlling liquid droplets and aggregates of proteins.
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