| Abstract: |
Gold nanoclusters (AuNC) are ultra small-sized entities (<3 nm)[1] exhibiting molecular-like electronic properties[2] and having intrinsic catalytic activity[3]. Characteristics of the stabilizing ligand of AuNC are critical because of the fact that they change the photoluminescence and catalytic properties of the AuNC by influencing the electron transfer mechanisms[4] and size distributions[5]. Proteins have been widely chosen as stabilizing ligands to maintain the biocompatibility and functionality of the AuNC in biological applications[6]. However, protein surface charge and folding are affected during the synthesis of AuNC via the bio-friendly synthesis route[7]. Therefore, it is pivotal to investigate the hydrodynamic properties of the protein-stabilized AuNC in real environmental conditions for further understanding of the biological activity and catalytic performance of the protein-stabilized AuNC.
Herein, we employed Multi-Wavelength Analytical Ultracentrifugation (MWL-AUC)[8] to reveal the molecular mass, shape factor, and hydration degree of bovine serum albumin (BSA) stabilized AuNC (AuNC@BSA) and genetically cysteine engineered Klentaq DNA Polymerase (KTQ5C) stabilized AuNC (AuNC@KTQ5C). Thereby, we had detailed insights into structural properties, enzymatic performance, and size of the protein-stabilized AuNC.
References
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