Factors affecting interactions between sulphonate-terminated dendrimers and proteins: A three case study

Colloids Surf B Biointerfaces. 2017 Jan 1:149:196-205. doi: 10.1016/j.colsurfb.2016.10.020. Epub 2016 Oct 11.

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.

Keywords: Computer modeling; Fluorescence; Molecular dynamics; Protein-dendrimer interaction; Quenching; Sulphonate-terminated carbosilane dendrimers.

MeSH terms

  • Animals
  • Cattle
  • Chickens
  • Dendrimers / chemistry*
  • Horses
  • Hydrogen-Ion Concentration
  • Isoelectric Point
  • Molecular Dynamics Simulation
  • Molecular Weight
  • Muramidase / chemistry*
  • Myoglobin / chemistry*
  • Serum Albumin, Bovine / chemistry*
  • Silanes / chemistry*
  • Spectrometry, Fluorescence
  • Static Electricity

Substances

  • Dendrimers
  • Myoglobin
  • Silanes
  • carbosilane
  • Serum Albumin, Bovine
  • Muramidase