Interaction of Atomically Precise Thiolated Copper Nanoclusters with Proteins: A Comparative Study

[Image: see text] A facile synthesis of glutathione-stabilized copper nanoclusters (CuNCs) is carried out in H(2)O/ tetrahydrofuran medium. The photophysical and morphological studies performed with as-synthesized CuNCs revealed the formation of green-emissive, stable, and smaller nanoclusters. The precise composition of these as-synthesized CuNCs was predicted with the aid of electrospray ionization mass spectrometry analysis as Cu(12)(SG)(9). Furthermore, the systematic studies of the interaction of synthesized CuNCs with three plasmatic proteins, namely, bovine serum albumin (BSA), lysozyme (Lys), and hemoglobin (Hb) have been performed by using a series of spectroscopic studies. The conformational changes in these proteins upon interacting with CuNCs and their binding stoichiometries have been investigated from the combination of UV–visible and steady-state fluorescence measurements. The changes in the microenvironment of proteins caused by CuNCs were investigated by circular dichroism spectroscopy. Among these three proteins, BSA and Lys had a minor effect on the luminescence of CuNCs, which makes them suitable candidates for biological applications. There are no drastic changes in the microenvironment of NCs as well as proteins because of the possibilities of weak electrostatic and H-bonding interactions of CuNCs with BSA and Lys. The feasibility of strong metallophic interaction between the Fe(2+) present in the heme group of Hb and Cu(I) or -S atoms present in the CuNCs brings considerable changes in the photophysical activity of CuNCs and their interactions with Hb. The functional groups on NCs as well as active amino acid residues present in proteins play a crucial role in determining their interactions. This work shed a piece of knowledge on designing NCs for specific biological applications.