Feasibility of cationic carbosilane dendrimers for sustainable protein sample preparation
[Display omitted] •Dimethylamino-terminated carbosilane dendrimers can form complexes with proteins.•Interactions depend on pH and dendrimer concentration and generation.•Pair generation (2 G and 4 G) dendrimers formed insoluble complexes with proteins.•These dendrimers were proposed for protein sam...
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Veröffentlicht in: | Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2020-02, Vol.186, p.110746-110746, Article 110746 |
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Sprache: | eng |
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•Dimethylamino-terminated carbosilane dendrimers can form complexes with proteins.•Interactions depend on pH and dendrimer concentration and generation.•Pair generation (2 G and 4 G) dendrimers formed insoluble complexes with proteins.•These dendrimers were proposed for protein sample preparation.•This proposal is more sustainable than usual methods that require organic solvents.
Protein sample preparation is the bottleneck in the analysis of proteins. The aim of this work is to evaluate the feasibility of carbosilane dendrimers functionalized with cationic groups to make easier this step. Anionic carbosilane dendrimers (sulphonate- and carboxylate-terminated) have already demonstrated their interaction with proteins and their potential in protein sample preparation. In this work, interactions between positively charged carbosilane dendrimers and different model proteins were studied when working under different pH conditions, dendrimer concentrations, and dendrimer generations. Amino- and trimethylammonium-terminated carbosilane dendrimers presented, in some cases, weak interactions with proteins. Unlike them, carbosilane dendrimers with terminal dimethylamino groups could interact, in many cases, with proteins and these interactions were affected by the pH, the dendrimer concentration, and the dendrimer generation. Moreover, dendrimer precipitation was observed at all pHs, although just second and fourth generation (2 G and 4 G) dendrimers resulted in the formation of complexes with proteins. Under experimental conditions promoting dendrimer-protein interactions, 2 G dimethylamino-terminated dendrimers were proposed as an alternative to other methods used in analytical chemistry or analysis in which an organic solvent or a resin are required to enrich/purify proteins in a complex sample. |
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ISSN: | 0927-7765 1873-4367 |
DOI: | 10.1016/j.colsurfb.2019.110746 |