Depending on the structure of the PBH capping ligand, the behaviour of AuNPs differed both in terms of stability and biocompatibility. The PBH-capped AuNPs used in this study check details associated in different ways, forming agglomerates of different sizes under culture conditions, as demonstrated through DLS measurements, UV–vis click here analysis and optical imaging. The stability of these particles over time is dictated by both the structure of the PBH ligand and the surrounding medium. Even the smallest of changes in ligand structure can lead to great differences in AuNP behaviour. We detected clear differences in the hydrodynamic size of AuNPs in EMEM/S+ and EMEM/S-. In the former, all the AuNP preparations experienced

a uniform increase in hydrodynamic size, possibly because see more of serum coating forming a corona, as proposed for

other NPs [54, 55], but these preparations remained in a stable size distribution over 24 h. It would appear that the serum coating prevented further interaction between the individual AuNPs over time. In agreement with this finding, Ehrenberg et al. [56] demonstrated protein binding to polystyrene particles (100 nm) with COOH functional groups within seconds with stable protein-coated NPs after as little as 30 min and these NPs remained stable for the entire test period (4 h). According to our UV–vis and DLS analyses, all PBH-capped AuNPs form stable agglomerates under culture conditions when serum was present. However, considerations are needed when

serum is not present. In this case, the structure of the PBH greatly influences the stability and biocompatibility of the AuNP. In EMEM/S-, the characteristic hydrodynamic size distribution profiles of all the NP preparations increased considerably in a time-dependent manner, with the exception of Au[(Gly-Tyr-TrCys)2B]. This PBH-capped AuNP had the same hydrodynamic size distribution profile range (150 to 260 nm) in EMEM/S- as in a water suspension and in medium containing serum. Thus, the hydrodynamic size decreased approximately 40 nm upon incubation. This reveals that the medium culture had less of an effect on the AuNPs Au[(Gly-Tyr-TrCys)2B]. Cobimetinib Interestingly, sizes up to micron scale were recorded for Au[(Met)2B] (1,568 nm) almost immediately upon contact with the EMEM/S- medium. UV–vis analysis of this AuNP suspension over time revealed red shifts in the SPR band, with a slight broadening, suggesting agglomeration of NPs in that medium. For Au[(Gly-Trp-Met)2B], Au[(Gly-Tyr-Met)2B] and Au[(Met)2B], which contain methionine, a minimal decrease in the intensity band was observed over time, probably caused by the adsorption of amino acids of the culture medium. In contrast, in the UV–vis spectrum of Au[(Gly-Tyr-TrCys)2B], the decrease in the intensity of SPR band was not observed, suggesting that the steric bulk and the strong interaction of (Gly-Tyr-TrCys)2B with the gold prevents the adsorption of compounds from culture medium.