Internalization of a Preformed Atomically Precise Silver Cluster in Proteins by Multistep Events and Emergence of Luminescent Counterparts Retaining Bioactivity
mediaposted on 22.11.2019 by Debasmita Ghosh, Mohammad Bodiuzzaman, Anirban Som, Sebastian Raja, Ananya Baksi, Atanu Ghosh, Jyotirmoy Ghosh, Akshayaa Ganesh, Priyanka Samji, Sundarasamy Mahalingam, Devarajan Karunagaran, Thalappil Pradeep
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A new synthetic protocol is introduced which preserves the secondary structure of protecting proteins encapsulating a luminescent atomically-precise silver cluster. This was achieved by using a preformed triphenylphosphine (TPP)-protected silver cluster as the precursor forming bovine serum albumin (BSA)- and human serum albumin (HSA)-protected Ag18 clusters. This is the first example of the formation of luminescent protein-protected clusters in a neutral medium, without using any reducing agent, which results in minimal alteration of the protein structure during cluster growth. The cluster formed showed exceptional stability, unlike other silver clusters of this class. The formation of these red luminescent clusters was visualized by UV–vis and photoluminescence spectroscopy. The identification of Ag18 core was made through matrix-assisted laser desorption ionization mass spectrometry (MALDI MS), and a plausible mechanism of the formation was identified by monitoring the systematic growth of the cluster core by time-dependent MALDI MS experiments and electrospray ionization mass spectrometry (ESI MS) of the reaction mixture. The cluster was successfully employed as a luminescent probe for cancer cell imaging. Retention of protein conformation in the clusters was confirmed through circular dichroism (CD) spectroscopy, and the same was reflected in the retention of 89% of the esterase activity of BSA in the Ag18@BSA clusters synthesized by this method, compared to only 28.7% for AgQC@BSA clusters synthesized using previous protocols, conducted in basic medium.