Abstract
The data provided in this paper are associated with the data in the «Binding of L-tryptophan and bovine serum albumin by novel gold nanoparticles capped with amphiphilic sulfonatomethylated calixresorcinarenes» paper (Shalaeva et al., 2019). Here, we represent i) the characterization data of calixresorcinarenes capped gold nanoparticles obtained by TEM and Vis- and IR spectroscopy; ii) the data giving the information about the interaction of modified AuNPs with L-tryptophan and bovine serum albumin by dynamic light scattering, spectrophotometry and fluorescence spectroscopy.
Highlights
Data on binding of L-tryptophan and bovine serum albumin by novel gold nanoparticles capped with amphiphilic sulfonatomethylated calixresorcinarenes
The data provided in this paper are associated with the data in the «Binding of L-tryptophan and bovine serum albumin by novel gold nanoparticles capped with amphiphilic sulfonatomethylated calixresorcinarenes» paper (Shalaeva et al, 2019)
We represent i) the characterization data of calixresorcinarenes capped gold nanoparticles obtained by Transmission electron microscopy (TEM) and Vis- and IR spectroscopy; ii) the data giving the information about the interaction of modified AuNPs with L-tryptophan and bovine serum albumin by dynamic light scattering, spectrophotometry and fluorescence spectroscopy
Summary
Chemistry Nanoparticles, calixresorcinarenes, protein Tables, microscopy images, graphs Spectrophotometry: Perkin Elmer Instruments TEM: Libra 120 IR: Bruker Vector 22 Fluorimetry: Varian Cary Eclipse DLS: Zetasizer Nano instrument Raw, analyzed, processed The nanoparticles were synthesized using calixresorcinarenes both as reducing and stabilizing agents in an aqueous solution at 25 C in the air atmosphere with stiring during 2 hours. The TEM images, DLS, spectrophotometry and fluorimetry data presented here confirmed the formation of hybrid systems on the base of gold nanoparticles and amphiphilic sulfonatomethylated calixresorcinarenes with controlled size, aggregation, electro-optical and binding properties and could be useful for the understanding of the interaction mechanisms between protein and nanoparticles, give information about structural and functional changes of BSA and the nanoparticles. This investigation has a value due to the promising possibility to use such systems for protein transport and visualization in biological media. The error of the hydrodynamic particle size determination was
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