According to recent literature, it is believed that the oligomeric form of amyloid beta (A?) is the leading cause of Alzheimer’s disease (1; 8; 10; 12-18). Additionally, recent studies have eluded to the impact of Alzheimer’s disease (AD) both economically and socially in today’s society where an increase of about 71% of AD related deaths were recorded between 2000 and 2013 (7). Since the oligomeric forms of A? vary in size, shape and some believe conformation, it is vital to utilize a separation technique, such as capilllary electrophoresis (CE) to further understand A? aggregation. By understanding A? aggregation, treatment of AD or preventive care measurements could be additionally developed. Therefore in this study, field amplified sample stacking (FASS) technique on the CE was utilized to provide higher resolution in oligomeric A?1-42 detection without causing significant changes to the aggregation. It was observed that the FASS technique provided smaller peak widths and increased peak heights on the CE compared to the non-FASS conditions. Furthermore by conducting thioflavin-t (ThT) assays, it was observed changing the buffer concentrations in accordance to the FASS technique conditions did not effect the overall aggregation. Thioflavin-t (ThT) assays were also conducted in order to determine an agitation rate where the oligomers of A?1-42 were observed on the CE. The oligomeric species observed were believed to be less than or equal to 100 kDa. Additionally, Congo red and Orange G inhibition were conducted to confirm oligomeric A?1-42 species were observed on the CE. Both inhibition studies alongside TEM imaging proved the aggregates observed on the CE in the 27 hour aggregation were smaller than proto-fibrils. Future work on natural compound inhibition studies using CE are recommended to see how those inhibitors target A?1-42 species that are less than or equal to 100 kDa.