The salt of HAuCl4 is commonly used in nanoparticle synthesis. Gold nanoclusters have strong fluorescence and biocompatibility and are widely used in molecular biology. Numerous proteins were reported as templates for nanocluster synthesis. More studies need to determine the properties of the appropriate proteins to this end. It is predictable in the nanoclusters' harsh conditions (alkaline pHs and high temperatures) the protein fold-state changes and forms aggregates. This study prepared the Au-NCs synthesis conditions to propose rhGH as a protein template, which had not been reported earlier. It was compared with the protein in the same condition without HAuCl4. The techniques used were UV-visible absorbance, fluorescence spectrophotometry, and DLS. Further investigation of the samples was done in the presence of different ions. Even though the measurements did not support the formation of nanoparticles, significant differences were observed in the aggregates of rhGH formed in the samples. The data showed that in contrast to the aggregates formed in the absence of HAuCl4, aggregates formed in the presence of HAuCl4 have a uniform population, various UV/Vis spectra, and different fluorescence behavior in response to the addition of ZnSO4. These findings display a small path in the big world of forming regular aggregates.