Many of the most widely used pesticides are aromatic, such as dichlorodiphenyltrichloroethane (DDT), atrazine, 2,4-dichlorophenoxyacetic acid, chlorothalonil, and azoxystrobin. Aromatic compounds are also commonly used as various drugs and dietary supplements, for example, 99% out of a dataset of 3,566 medicinal compounds were found to contain aromatic rings. The ability of the coacervates to encapsulate various aromatic compounds was investigated. The coacervates were shown to successfully encapsulate ThT, Rhodamine B (RhB), and crystal violet (CV) (Figure ). These dyes were chosen specifically for their resemblance to compounds that can be encapsulated inside the coacervates for applications such as drug delivery and biosensing. ThT is a benzothiazole salt. Benzothiazole is used on its own as a food additive, and its derivatives may be found in various drugs such as riluzole, lubeluzole, and ethoxazolamide. On the other hand, RhB and CV are dyes commonly used in the textile industry and as indicators. Thus, they are relevant for manufacturing sensors. The fluorescence intensity originating from these dyes inside the coacervates was significantly higher than in solutions without the peptide, indicating efficient partitioning (Figure ). The ability of the four peptides to encapsulate RhB was compared at pH 7.4 (Figure ). At this pH pep1 is zwitterionic, pep2 is cationic, pep3 is nonionic and pep4 is anionic. The anionic pep3 showed better partitioning capabilities of RhB than the cationic pep2, which is expected due to the repelling cationic charge of RhB. Other than that, the peptides behaved similarly, indicating that the charge screening from the salt ions negates the effects of the charge of the peptides on their ability to encapsulate. This behavior can also be observed when comparing the RhB partitioning ability of pep1 at different pH values. In this case, even though the net charge of the peptide increases when the pH decreases, the partitioning efficiency is increased (Figure ). Figure shows that the coacervation capabilities of pep1 during evaporation are greater at lower pH values. This indicates that the determining factor for the dye partitioning is not the charge of the peptide, but its ability to form coacervates as demonstrated in the phase diagrams.