In silico analysis of the interaction of de novo peptides derived from Salvia hispanica with anticancer targets.

Cancer is one of the leading causes of death worldwide. Conventional cancer therapies are not selective to cancer cells resulting in serious side effects on patients. Thus, the need for complementary treatments that improve the patient's response to cancer therapy is highly important. To predict and evaluate the physicochemical characteristics and potential anticancer activity of the peptides identified from S. hispanica protein fraction <1 kDa through the use of in silico tools. Peptides derived from Salvia hispanica's protein fraction <1 kDa were identified and analyzed for the prediction of their physicochemical properties. The characterized peptide sequences were then submitted to a multi-criteria decision analysis to identify the peptides that possess the characteristics to potentially exert anticancer activity. Through molecular docking analysis, the potential anticancer activity of the Potentially Anticancer Peptide (PAP)-1, PAP-2, PAP-3, PAP-4, and PAP-5 was estimated by their binding interactions with cancer and apoptosis-related molecules. All five evaluated PAPs exhibited strong binding interactions (< -100 kcal/mol). However, PAP-3 showed the lowest binding free energies with several of the targets. Thus, PAP-3 shows potential to be used as a nutraceutical or ingredient for functional foods that adjuvate in cancer treatment. Conclusions: Through the molecular docking studies, the binding of the PAPs to target molecules of interest for cancer treatment was successfully simulated, from which PAP-3 exhibited the lowest binding free energies. Further in vitro and in vivo studies are required to validate the predictions obtained by the in silico analysis.Communicated by Ramaswamy H. Sarma.

Antibacterial peptide fractions from chia seeds (Salvia hispanica L.) and their stability to food processing conditions.

Foodborne pathogens are one of the major causes of food deterioration and a public health concern worldwide. Antimicrobial peptides (AMPs) encrypted in protein sequences from plants, such as chia (Salvia hispanica), might have a crucial role in the inhibition of bacteria. In this study, the antibacterial activity and stability of chia peptide fractions (CPFs) were evaluated for potential applications in food preservation. Three CPFs (F < 1, F 1-3, and F 3-5 kDa) were obtained by enzymatic hydrolysis of a protein-rich fraction and subsequent ultrafiltration. Gram-positive bacteria were susceptible to F < 1. This fraction's more significant inhibition effect was reported against Listeria monocytogenes (635.4 ± 3.6 µg/mL). F < 1 remained active after incubation at 4-80 °C and a pH range of 5-8 but was inactive after exposure to pepsin and trypsin. In this sense, F < 1 could be suitable for meat and dairy products at a maximum reference level of 12-25 mg/kg. Multicriteria analysis suggested that KLKKNL could be the peptide displaying the antimicrobial activity in F < 1. These results demonstrate the potential of this sequence as a preservative for controlling the proliferation of Gram-positive bacteria in food products.