Factors affecting interactions between sulphonate-terminated dendrimers and proteins: A three case study
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články
PubMed
27764689
DOI
10.1016/j.colsurfb.2016.10.020
PII: S0927-7765(16)30724-X
Knihovny.cz E-zdroje
- Klíčová slova
- Computer modeling, Fluorescence, Molecular dynamics, Protein-dendrimer interaction, Quenching, Sulphonate-terminated carbosilane dendrimers,
- 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
- Názvy látek
- carbosilane MeSH Prohlížeč
- dendrimery MeSH
- muramidasa MeSH
- myoglobin MeSH
- sérový albumin hovězí MeSH
- silany 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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