The present study was designed to investigate the in vitro effect of purpurin on C. dubliniensis biofilms, with special attention on its correlation to cell demise. The main etiopathologic role of biofilms in pathogenic Candida fungi is its ability to maintain a community of invasive fungal population that serves as a reservoir for recurrent host infection and disease dissemination. Similar to its phylogenetically closely related species C. albicans, C. dubliniensis forms true hyphae and biofilms on both abiotic and biotic surfaces. The increasing clinical prevalence of C. dubliniensis as an emerging human fungal pathogen is reflected by an astonishing number of reports in detecting bloodstream isolates and medical devices such as catheters and implanted materials. Our laboratory recently deciphered the mechanisms of action of purpurin against Candida fungi through perturbation of mitochondrial homeostasis and initiation of apoptosis. More experiments indicated that purpurin also interferes with C. albicans biofilm development at sub-MIC levels. In the present study, we explored the antifungal activity of purpurin on biofilms and evaluated several biochemical hallmarks of cell demise, an area that is still relatively unexplored in this Candida species. The antifungal activity of purpurin on biofilms was evaluated semi-quantitatively by using XTT Chamigrenal reduction assay. The inhibitory effect was concentration dependent, as revealed by a progressive reduction in cell viability with increasing concentrations of purpurin. This is an entirely new antifungal action mechanism which is different from the standard antifungal agents in clinical settings: flucytosine inhibits DNA synthesis; polyenes cause membrane damage; azoles affect sterol metabolism; and echinocandins inhibit cell wall synthesis. In conclusion, the findings of the present study provide solid evidence that purpurin triggered apoptosis-like features in C. dubliniensis biofilms. As C. dubliniensis and C. albicans belong to the CTG clade, it is not surprising that they share common core pathways in metabolism. Nonetheless, a comparative analysis of calcineurin signalling pathways between C. dubliniensis and C. albicans indicated differential scenarios in pH homeostasis. Another study revealed a rewiring of iron assimilation gene expression in C. dubliniensis. Thus, comparing metabolic pathways between these two species not only helps gain further insights into their evolutionary divergence, but also alludes to a functional characterization of core machineries responsible for their pathogenicity. For instance, a better understanding of the cell death mechanisms can be beneficial to the design of innovative antifungal strategies that target the core components specifically. Anti-carbamyl-lysine antibodies have been in use for many years. We used a commercially available anti-carbamyl-lysine antibody to address whether carbamylated proteins are present in the kidneys of rats. As a preliminary confirmation of the specificity of the antibody, we incubated bovine serum albumin with urea for two to four days and immunoblotted the samples. After urea Isochlorogenic-acid-C incubation, the antibody recognized bovine serum albumin both as a monomer as well as in higher molecular weight complexes. In contrast, lanes loaded with samples prepared without urea did not show these bands. This result is compatible with the manufacturer’s data pointing to specificity of this antibody for carbamylated proteins. We used this antibody to probe immunoblots of rat renal cortex, outer medulla, and inner medulla. As hypothesized, many bands were seen in the inner medulla, consistent with the view that multiple carbamylated proteins are present in the inner medulla.