Abstract
An easily synthesizable pyrene-based amphiphilic probe (Pybpa) has been developed, which exhibited no responses with metal ions in the pure aqueous medium despite possessing a metal ion-chelating bispicolyl unit. We believe that spontaneous aggregation of Pybpa in aqueous medium makes the ion binding unit not accessible to the metal ions. However, the sensitivity and selectivity of Pybpa toward Zn2+ ions drastically improve in the presence of serum albumin protein, HSA. The differences in the microenvironment inside the protein cavity, in terms of local polarity, and conformational rigidity might be attributing factors for that. The mechanistic investigations also suggest that there might be the involvement of polar amino acid residues that take part in coordination with Zn2+ ions. Pybpa shows no detectable spectroscopic changes with Zn2+ ions in aqueous medium in the absence of HSA. However, it can effectively recognize Zn2+ ions in the protein-bound form. Moreover, the photophysical behavior of Pybpa and its zinc complex have been investigated with DFT and docking studies. Noteworthy, such an unusual sensing aspect of Zn2+ exclusively in the protein-bound state and particularly in aqueous medium is truly rare and innovative.
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