Short peptide-grafted interfaces regulate protein cluster coacervation
Phys. Rev. E 114, 015404 – Published 7 July, 2026
DOI: https://doi.org/10.1103/t3y7-qqqn
Abstract
The behavior of protein condensates driven by weak multivalent interactions has been extensively studied in bulk systems, yet their interfacial behavior remains far less explored. Using coarse-grained simulations, we investigated protein clusters adsorbed onto interfaces grafted with short peptides through weak multivalent interactions. We found that interface-mediated coarsening and fusion significantly enhance the coacervation of clusters into condensates. Moreover, the mobility of the grafted peptides plays a key role in determining condensate behavior: On interfaces with immobile peptides, increasing surface coverage drives a transition from dewetting to partial wetting, whereas on interfaces with mobile peptides, partial wetting is more likely to occur. Importantly, the weak protein-interface interactions do not impair the dynamic molecular exchange between the condensates and the surrounding solution. Our study provides valuable insights into how protein condensates behave at biological interfaces.
