ArticlePolymers2021
Deciphering the Role of π-Interactions in Polyelectrolyte Complexes Using Rationally Designed Peptides.
Article in Polymers, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Developing Design Rules for Polyelectrolyte Complex Materials: Role of Polyelectrolyte Length, Charged Group, and Backbone.Macromolecules · 2026Article
- Development of Amorphous Solid Dispersion to Improve the Dissolution and Antiproliferative Activity of Brazilin.Drug design, development and therapy · 2026Article
- Role of Charge Patterning and Hydrophobicity in Peptide-Based Complex Coacervates.Biomacromolecules · 2025Article
- Effect of Cation-π Interactions on the Phase Behavior and Viscoelastic Properties of Polyelectrolyte Complexes.Macromolecules · 2025Article
- Antioxidant and Anti-Obesity Properties of Acidic and Alkaline Seaweed Extracts Adjusted to Different pH Levels.Marine drugs · 2025Article
- Design Rules for the Sequestration of Viruses into Polypeptide Complex Coacervates.Biomacromolecules · 2024Article
- Self-Assembling Polypeptides in Complex Coacervation.Accounts of chemical research · 2024Article
- J-aggregation of 5, 10, 15, 20-tetraphenyl-21H, 23H-porphinetetrasulfonic acid in a molecular crowding environment simulated using dextran.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2022Article
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Authors and funding
3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Electrostatic interactions, and specifically π-interactions play a significant role in the liquid-liquid phase separation of proteins and formation of membraneless organelles/or biological condensates. Sequence patterning of peptides allows creating protein-like structures and controlling the chemistry and interactions of the mimetic molecules. A library of oppositely charged polypeptides was designed and synthesized to investigate the role of π-interactions on phase separation and secondary structures of polyelectrolyte complexes. Phenylalanine was chosen as the π-containing residue and was used together with lysine or glutamic acid in the design of positively or negatively charged sequences. The effect of charge density and also the substitution of fluorine on the phenylalanine ring, known to disrupt π-interactions, were investigated. Characterization analysis using MALDI-TOF mass spectroscopy, H NMR, and circular dichroism (CD) confirmed the molecular structure and chiral pattern of peptide sequences. Despite an alternating sequence of chirality previously shown to promote liquid-liquid phase separation, complexes appeared as solid precipitates, suggesting strong interactions between the sequence pairs. The secondary structures of sequence pairs showed the formation of hydrogen-bonded structures with a β-sheet signal in FTIR spectroscopy. The presence of fluorine decreased hydrogen bonding due to its inhibitory effect on π-interactions. π-interactions resulted in enhanced stability of complexes against salt, and higher critical salt concentrations for complexes with more π-containing amino acids. Furthermore, UV-vis spectroscopy showed that sequences containing π-interactions and increased charge density encapsulated a small charged molecule with π-bonds with high efficiency. These findings highlight the interplay between ionic, hydrophobic, hydrogen bonding, and π-interactions in polyelectrolyte complex formation and enhance our understanding of phase separation phenomena in protein-like structures.
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