Factors affecting interactions between sulphonate-terminated dendrimers and proteins: A three case study
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Updated: Mar 13, 2026

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
Published on: August 20, 2018
Estefanía González-García1, Marek Maly2, Francisco Javier de la Mata3
1Departamento de Química Analítica, Química Física e Ingeniería Química, Universidad de Alcalá, Ctra. Madrid-Barcelona Km. 33.600, 28871 Alcalá de Henares (Madrid), Spain.
Abstract:
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.
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