Our study provides valuable insights into the role of protein acetylation, exemplified by the acetylation of β-conglycinin, in modulating cellular signaling pathways relevant to inflammation and immune responses. By successfully acetylating β-conglycinin, a model protein rich in lysine residues, we have demonstrated the feasibility of modifying lysine residues within a protein structure and have discussed potential implications for NF-κB-mediated signaling pathways. This underscores the significance of post-translational modifications, such as acetylation, in regulating the activity and function of key transcription factors like NF-κB. Through the use of Aspirin-NHS to selectively acetylate lysine, we have shed light on how aspirin and related compounds may modulate NF-κB signaling and subsequent inflammatory responses. This research may have implications for personalized treatment strategies and preventive medicine approaches aimed at mitigating inflammatory diseases. Overall, our study contributes to a be er understanding of the molecular mechanisms underlying protein acetylation dynamics and its role in regulating cellular signaling pathways involved in inflammation, immunity, and disease. Future research efforts should focus on elucidating the specific molecular targets and mechanisms through which protein acetylation influences NF-κB-mediated signaling, with the ultimate goal of developing targeted therapeutic interventions for inflammatory disorders.