Work

Continuous phase hydrophobicity exerts substantial influence on the surface functional group prevalence in protein nanocapsules synthesized in inverse miniemulsion

Year: 2025
Type: article
Abstract: the click reaction between hydrophilic azide-modified proteins and a hydrophobic dialkyne crosslinker. By adjusting the solvent mixture of toluene and cyclohexane, the interfacial properties of the droplets are modified, influencing the partial denaturation of the protein and orientation of the amine-terminated lysine residues. This, in turn, affects the accessibility of the azide groups for the crosslinking. Changes in solvent composition furthermore influence the solubility and reactivity of the crosslinker, thereby modulating the degree of azide functionalization. This allows for precise control over the number of unreacted azide groups available for subsequent biorthogonal click reactions. We demonstrate that the multifunctional surface, with amine, azide and alkyne groups, enables the simultaneous attachment of different molecules to the nanocapsule. Finally, we show that while changes in continuous phase hydrophobicity lead only to minor changes in protein corona composition, they significantly affect macrophage uptake, likely due to differences in surface amine density. Our combined findings provide a novel approach for tailoring the surface functionality of nanocapsules, facilitating more precise and versatile biofunctionalization strategies, particularly for targeted drug delivery.
Language: English
Subfield: Biomaterials
Open Access status: hybrid
OpenAlex ID: W4416132173
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Cites: 31
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