This work proposes a deep study on the interactions between sulphonate-terminated carbosilane dendrimers and proteins. Three different proteins with different molecular weights and isoelectric points were employed and different pHs, dendrimer concentrations and generations were tested. Variations in fluorescence intensity and emission wavelength were used as protein-dendrimer interaction probes. Interaction between dendrimers and proteins greatly depended on the protein itself and pH. Other important issues were the dendrimer concentration and generation. Protein-dendrimer interactions were favored under acidic working conditions when proteins were positively charged. Moreover, in general, high dendrimer generations promoted these interactions. Modeling of protein-dendrimer interactions allowed to understand the different behaviors observed for every protein.

• MeSH
• dendrimery chemie   MeSH
• fluorescenční spektrometrie MeSH
• izoelektrický bod MeSH
• koncentrace vodíkových iontů MeSH
• koně MeSH
• kur domácí MeSH
• molekulová hmotnost MeSH
• muramidasa chemie   MeSH
• myoglobin chemie   MeSH
• sérový albumin hovězí chemie   MeSH
• silany chemie   MeSH
• simulace molekulární dynamiky MeSH
• skot MeSH
• statická elektřina MeSH
• zvířata MeSH
• Check Tag
• skot MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH

Protein sample preparation is a critical and an unsustainable step since it involves the use of tedious methods that usually require high amount of solvents. The development of new materials offers additional opportunities in protein sample preparation. This work explores, for the first time, the potential application of carboxylate-terminated carbosilane dendrimers to the purification/enrichment of proteins. Studies on dendrimer binding to proteins, based on protein fluorescence intensity and emission wavelengths measurements, demonstrated the interaction between carboxylate-terminated carbosilane dendrimers and proteins at all tested pH levels. Interactions were greatly affected by the protein itself, pH, and dendrimer concentration and generation. Especially interesting was the interaction at acidic pH since it resulted in a significant protein precipitation. Dendrimer-protein interactions were modeled observing stable complexes for all proteins. Carboxylate-terminated carbosilane dendrimers at acidic pH were successfully used in the purification/enrichment of proteins extracted from a complex sample. Graphical Abstract Images showing the growing turbidity of solutions containing a mixture of proteins (lysozyme, myoglobin, and BSA) at different protein:dendrimer ratios (1:0, 1:1, 1:8, and 1:20) at acidic pH and SDS-PAGE profiles of the corresponsing supernatants. Comparison of SDS-PAGE profiles for the pellets obtained during the purification of proteins present in a complex sample using a conventional "no-clean" method based on acetone precipitation and the proposed "greener" method using carboxylate-terminated carbosilane dendrimer at a 1:20 protein:dendrimer ratio.

• MeSH
• chemická precipitace MeSH
• dendrimery chemie   MeSH
• koncentrace vodíkových iontů MeSH
• kyseliny karboxylové chemie   MeSH
• muramidasa chemie   izolace a purifikace   MeSH
• myoglobin chemie   izolace a purifikace   MeSH
• rostlinné proteiny izolace a purifikace   MeSH
• rozpouštědla MeSH
• sekundární struktura proteinů MeSH
• semena rostlinná chemie   MeSH
• sérový albumin hovězí chemie   izolace a purifikace   MeSH
• silany chemie   MeSH
• simulace molekulární dynamiky MeSH
• slivoň švestka chemie   MeSH
• vazba proteinů MeSH
• Publikační typ
• časopisecké články MeSH