Interplay of Hydrophobicity, Charge, and Sequence Length in Oligopeptide Coassembly
Year: 2025
Type: article
Abstract: Peptide coassembly offers novel opportunities for designing advanced nanomaterials. This study used coarse-grained molecular dynamics simulations to examine the coassembly of charge-complementary peptides, assessing various ratios and the role of charge and hydrophobicity in their aggregation. We discovered that peptide length, charge, and hydrophobicity significantly influence coassembly behavior, with more hydrophobic peptides exhibiting greater aggregation despite electrostatic repulsion. Beyond the coassembly of two peptides, we also observed that the coassembly of more than two peptides will likely lead to new assembly structures and properties. Our findings underscore the importance of peptide composition and length in tuning the coassembly and the resulting properties, thus facilitating the design of complex peptide nanoparticles for biomedical and biotechnological applications.
Institution: Purdue University West Lafayette
Language: English
Subfield: Biomaterials
Field: Materials Science
Domain: Physical Sciences
Open Access status: green
OpenAlex ID: W4409726356