Pancreatic cancer accounts for about 7% of all cancer deaths. The ability for aggressive metastatic progression as well as the asymptomatic disease development and a lack of inadequate detection methods result in a low survival rate of about 3%. However, peptides with high affinity and specificity show promise as radiolabeled imaging agents for both detection and therapy. Previously, we used phage display technology to identify a peptide, MCA1, that binds to the human ductal adenocarcinoma pancreatic cell line, Mia Paca-2 while showing no binding to other cancerous and non-cancerous cell lines (LNCaP, HEK293, hTERT-HPNE, and SKOV-3). Here, the pancreatic cancer cell line specificity of MCA1 was further elucidated. A dose-response assay using a modified ELISA was used to determine the EC50-values of MCA1 to Mia Paca-2, metastatic ductal adenocarcinoma (CFPAC-1), primary adenocarcinoma (Panc 10.05), and ascitic adenocarcinoma (HPAF-II) cells. The EC50-values were calculated to be 299.0 nM (248.3-359.7 nM; 95% confidence interval; CI), 1.24 µM (0.167-73.93 µM 95% CI), 51.69 µM (1.28 µM -undetermined 95% CI), and 24.22 µM (3.00-275 µM 95% CI), respectively. The R2-values for the sigmoidal dose-response curves were 0.9376, 0.2172, 0.5663, and 0.3096 for Mia paca-2, CFPAC-1, Panc 10.05, and HPAF-II cells, respectively. These results show that MCA1 exhibits the highest affinity to the original target cell line (Mia Paca-2) and shows comparatively low binding with wide 95% CI and low R2-values to the other cell lines. This indicates that the peptide is specific for the Mia Paca-2 cells and may target a biomarker not expressed in CFPAC-1, Panc 10.05, and HPAF-II cells. Thus, MCA1 may be further developed as a specific ligand of subtypes of pancreatic ductal adenocarcinoma.

Pancreatic cancer specificity of phage display-selected peptide MCA1

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