From literature, it could be observed that while binding of gold nanoparticle and protein occurs the UV-VIS peak of gold shifts by a small amount suggesting binding. Although further characterization is required for binding, this serves as a preliminary test. In the same way, for release of proteins will the shifted peak come back to the old gold peak? Have anyone characterized preliminarily through UV Vis regarding the unbinding? Thanks in advance for everyone's time to answer this question
The protein nanoparticle interaction is very strong, when proteins in contact with nanoparticles results into formation of soft and hard corona, protein release/exchange occures only in case of soft corona. when we consider UV visible reading, red shift occurs as a result binding, but it would not be possible to remove all bound proteins, because the reaction is spontaneous. It may be possible that gold nanoparticle may not show its original peak. Instead of Uv visibl, you can use fluorescense spectrometer for the same.
when the spectrum of gold nanoparticle didnot change there is no binding.
when the gold binding with protein the peak must be have red shift and the intensity must be decreased and appear a new peak because of the aggregation process.
In principle gold nanoparticle peak must be observed. But in practice total unbinding is not possible, so getting original gold peak may not be possible. Certainly one can get clear picture through fluorescence spectroscopy.
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