Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets

[Image: see text] Proteins possess various domains and subdomain pockets with varying hydrophobicity/hydrophilicity. The local polarities of these domains play a major role in oxidation–reduction-based biological processes. Herein, we have synthesized ultrasmall fluorescent copper nanoclusters (Cu NCs) that are directed to bind to the different domain-specific pockets of the model protein bovine serum albumins (BSA). Potential electron acceptors, methyl viologen (MV) derivatives, were chosen such that they specifically reach the various domains following their hydrophobicity/hydrophilicity. Here, we have used MV(2+), HMV(+), and DHMV(2+), possessing hydrophilic, intermediate, and hydrophobic specificities. Being electron acceptors, these derivatives draw electrons from the Cu NCs through photoinduced electron transfer (PET). The rate of PET varies at the different domains of BSA based on the local environment which has been analyzed. Here, PET is confirmed by steady state as well as time-resolved fluorescence spectroscopy. This study would provide a measurable way to identify the location of the different domains of a protein which is scalable by changing the superficial conditions without unfolding the protein.