Size Evolution of Protein-Protected Gold Clusters in Solution: A Combined SAXS-MS Investigation

Abstract

We report a combined small-angle X-ray scattering (SAXS) and mass spectrometric (MS) study of the growth of gold clusters within proteins, in the solution state. Two different proteins, namely, lysozyme (Lyz) and bovine serum albumin (BSA), were used for this study. SAXS study of clusters grown in Lyz shows the presence of a 0.8 nm gold core, which is in agreement with the Au-10 cluster observed in MS. Dynamic light scattering suggests the size of the cluster core to be 1.2 nm. For BSA, however, a bigger core size was observed, comparable to the Au-33 core obtained in MS. Concentration- and time-dependent data do not show much change in the core size in both SAXS and MS investigations. When metal-protein adducts were incubated for longer time in solution, nanoparticles were formed and protein size decreased, possibly due to the fragmentation of the latter during nanoparticle formation. The data are in agreement with dynamic light scattering studies. This work helps to directly visualize cluster growth within protein templates in solution.