NF-κB plays a pivotal role in regulating the expression of genes involved in inflammation, immunity, cell survival, and proliferation. By acetylating β-conglycinin, which shares lysine-rich motifs with NF-κB, insights can be gained into how acetylation influences the transcriptional activity of NF-κB. The study was conducted in a similar cellular environment and therefore acetylating β-conglycinin in these conditions can allow us to gain insights into the effects of aspirin-mediated acetylation. Acetylation of proteins can lead to their inhibition and in the context of carcinogenesis, this inhibition can be vital . Acetylation of NF-κB shows promise as a potential way to modulate its specific signaling and inflammatory responses. Selective lysine acetylation on the protein is not only feasible, but could potentially be beneficial in inhibiting NF-κB. The inhibition of NF-κB is associated with improved patient outcomes, so a method of selective acetylation can be valuable in this context . The successful acetylation of β-conglycinin validates the feasibility of modifying lysine residues within a protein structure and provides a platform for studying the effects of acetylation on protein function.