Our studies revolve around the anthrax which is a rare but serious infectious disease caused by Bacillus anthracis bacterium. The anthrax toxin is composed of protective antigen (PA), edema factor (EF), and lethal factor (LF). LFn corresponds to the N-terminal domain at which LF binds to PA, allowing for the formation of lethal toxin (LT). LT binding to dendritic cells leads to a defective immune response and ultimately host death. Earlier studies that investigated the native to unfolded state of LFn using Guanidine HCl as a denaturant found that a decrease in pH (7.5-4) led to a drop in initial fluorescence intensity. Our research investigates an alternate state of LFn in which it becomes aggregated at low pH. To further understand the factors that prevent or promote aggregation in LFn, we have completed an array of experiments which utilize elastic light scattering to measure aggregation of LFn when refolding using denaturant solutions. Analyzing the kinetics of light scattering can provide insight on the rate of aggregation, where we were able to make a conclusion about the promotion or prevention of aggregation considering varying pHs of urea, different denaturants (guanidine HCl (GdnHCl)), and the salts NaCl and choline chloride. Our findings indicate that a higher degree of aggregation is observed at pH 5 rather than pH 8 when refolding in urea. When using GdnHCl as a denaturant, the data showed little to no aggregation at pH 5. We hypothesized that this could be due to the salt effects of guanidine HCl, but when using urea with salts such as NaCl and choline chloride (0.9 M) no decrease in aggregation was observed. This affirms our conclusion that guanidine is an exceptional denaturant when considering preventing further aggregation. Our future studies will focus on measuring refolding of LFn at low pH using guanidine HCl.