Factors affecting interactions between sulphonate-terminated dendrimers and proteins: A three case study
Language English Country Netherlands Media print-electronic
Document type Journal Article
PubMed
27764689
DOI
10.1016/j.colsurfb.2016.10.020
PII: S0927-7765(16)30724-X
Knihovny.cz E-resources
- Keywords
- Computer modeling, Fluorescence, Molecular dynamics, Protein-dendrimer interaction, Quenching, Sulphonate-terminated carbosilane dendrimers,
- MeSH
- Dendrimers chemistry MeSH
- Spectrometry, Fluorescence MeSH
- Isoelectric Point MeSH
- Hydrogen-Ion Concentration MeSH
- Horses MeSH
- Chickens MeSH
- Molecular Weight MeSH
- Muramidase chemistry MeSH
- Myoglobin chemistry MeSH
- Serum Albumin, Bovine chemistry MeSH
- Silanes chemistry MeSH
- Molecular Dynamics Simulation MeSH
- Cattle MeSH
- Static Electricity MeSH
- Animals MeSH
- Check Tag
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- carbosilane MeSH Browser
- Dendrimers MeSH
- Muramidase MeSH
- Myoglobin MeSH
- Serum Albumin, Bovine MeSH
- Silanes MeSH
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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