Biophysical Study of the Potential Antitumoral Activity of NA-CATH-ATRA-1-ATRA-1 with Model Membranes

Breast cancer is the most commonly diagnosed cancer in women in both developed and developing countries. Due to the increasing alarms in the detection of cases every year, it is considered a priority to evaluate new molecules as potential antitumoral agents. Among these molecules, cationic peptides have emerged as promising therapeutic agents with a membrane-based mechanism of action very hard to counteract by the cancer cells. This biophysical study seeks to offer preliminary insights into how NA-CATH:ATRA-1-ATRA-1, a synthetic cationic peptide derived of the peptide NA-CATH, isolated from the species Natra aja or Chinese cobra, is a potential antitumoral compound at the membrane level on breast cancer cell lines. The interaction of the NA-CATH-ATRA-1-ATRA-1 with two lipid systems representative of tumoral and non-tumoral membranes was followed by differential scanning calorimetry and Fourier-transform infrared spectroscopy. The results showed a strong interaction of NA-CATH-ATRA-1-ATRA-1 with the lipids present in the eukaryotic membranes, especially phosphatidylserine, suggesting a mechanism based on the electrostatic interaction of the peptide with the anionic lipids of the tumoral cancer membranes. The biophysical studies are essential to understand the mechanism of action of a potential pharmaceutics.

NA-CATH-ATRA-1-ATRA-1; breast cancer; lipid–peptide interactions; differential scanning calorimetry; Fourier-transform infrared spectroscopy