PNC-27- 5MG

PNC-27

PNC-27 is a peptide consisting of 27 amino acids which has been researched in order to reduce the function and multiplication of cancer cells. The third helix of the Well antisarcoma peptide α-helical segment of p53 (ASPP2), a protein known as tumor suppressors. Cell Annihilation by Necrosis Inducers PNC-27 has been shown to promote cell death in different cancer cell lines such as pancreatic cancer, ovarian carcinoma, leukemia and others.

The PNC-27 peptide has intrigued researchers, who believe that it can selectively target cancer cells without apparently binding to the other cells. The history of this peptide dates to the year 2000 and was first synthesized for a research project which related to immunodeficiency, specifically HIV, as it had been reported that this peptide had the property to bind with a membrane protein called Double Minute (HDM2), which is believed to be over-expressed on these membranes of carcinogenic cells. Fortunately, PNC-27 does not appear to trigger apoptosis (which as we know is a common route for most anti-cancer compounds) and instead may work on these cells by deadening them via necrosis. The mode of action of these proteins is consistent with a direct, physical disruption of the plasma membrane - conceivably via pore formation that causes loss of cellular integrity and necrosis. Collectively, binding to this protein seems lysis or holes in the cancer cell membrane creating membranolysis. Ion movements from extracellular solution to cytosol, and vice versa, trigger influx of ions into the cell and outflow of cellular contents, respectively until the cells dies.

A second study (Niemiwa et al., 2010) also tested pore-forming activity of the whole peptide, its fragments and parts of the sequence in 2010 as well. The premise was that, if left intact, the peptide might better facilitate membranolysis-the process by which cancer cells are killed. In this study, the peptide was labeled with a green fluorescence compound at the amino-group-carrying terminal and with a red fluorescence compound at the carboxyl-group-carrying terminal. The labeling technique was critical, as it enabled the researchers to see how intact the peptide remained within cells. The color of the membrane during membranolysis was detected after the breast tumor and control cells were treated by exposing them to the modified peptide. When the cells were lysed, a bright yellow luminescence was detected half an hour after treatment with the peptide, indicating that the peptide was completely intact during this process of cellular membrane killing. This was important to observe as it indicated that the form of the peptide was retained during interaction with the cell membrane, which would be required for any cytotoxic function. As anticipated; only the cancerous cells died due to this, while the control ncells survive. The researchers of the study say that PNC-27, being a peptide, only seems to cause pore development on cancer cell membranes which might be necessary for its activity and related with the release of lactate dehydrogenase (LDH), a marker of cell lysis. The correlation with increasing LDH release and viability suggested that PNC-27 interaction with cancer cell membranes rose across time, which increased the killing effect. Kelley A. Sookraj et al. stated,

PNC-27-mediated cancer cell membrane lysis in identity to the unmodified peptide, not peptides from fragmentation. The diffuse green fluorescence is from PNC-27 interacting with normal membrane while the punctate yellow fluorescence represents how PNC-27 interacts with intramembrane target of MCF-7 cells compared to the untransformed cell line. This interaction prolongs the half-life of PNC-27. Initial, the double-labeled peptide is homogenously fluorescent in the membranes of untransformed MCF-10-2A cells since these targets are absent on their membranes whereupon the cells degrade easily the double-labeled peptide.

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