Helicobacter pylori is the most common cause of peptic ulcers and gastroduodenal pathologies and has been identified by the World Health Organization as a serious threat to human health. The increasing antibiotic resistance of H. pylori necessitates prevention and early intervention, as well as the discovery of novel drugs. Amaranth, chia, and quinoa are classified as pseudocereals and are known as superfoods because of their nutritional density. The effect of consuming these pseudocereals at the onset of H. pylori infection was investigated using in silico methods. 34 proteins from amaranth, chia, and quinoa were subjected to in silico pepsin digestion, and antimicrobial, antibiofilm, and cell-penetrating activities of the released peptides were analyzed. Peptides predicted to be cell-penetrating were further used for peptide-protein docking. 58 peptides were predicted to have antimicrobial activity whereas 76 were predicted to have antibiofilm activity. A total of 116 peptides were classified as cell-penetrating peptides, and those with the highest scores were used for peptide-protein docking with shikimate dehydrogenase, type II dehydroquinase, and D-alanine-D-alanine ligase of H. pylori to evaluate their enzyme inhibition potential. A peptide released from the chia seed proteins A0A1Z1EC55 and A0A1Z1EC46 with the sequence SWKYSHRRHHSNTGSL gave the highest docking energy scores for all three enzymes. To the best of our knowledge, this is the first work concerning the effect of ingested food on H. pylori infection. We believe our results will provide valuable data and a new point of view for the scientists interested in this topic.

HIGHLIGHTS

• H. pylori is a common infection and the leading cause of gastroduodenal pathologies.
• Gastric digestion of amaranth, chia, and quinoa proteins with pepsin revealed antimicrobial and antibiofilm peptides that may be effective against H. pylori growth.
• One particular peptide SWKYSHRRHHSNTGSL had high docking energy scores when docked to the three enzymes of H. pylori.

Cyanobacterial peptides are a group of promising natural therapeutic agents that have been extensively studied in recent years. They can be valuable pharmaceuticals or lead compounds in developing novel therapeutics for various diseases, especially cancers, infections, and neurodegenerative diseases, which are the most important challenges of medicine today.

HIGHLIGHTS

• Cyanobacteria are a valuable source of natural metabolites, including bioactive peptides.
• Cyanobacterial peptides include ribosomal synthesized and nonribosomal peptides (NRPs).
• Therapeutic applications of cyanobacterial peptides in different diseases have been reported.

Cyanophycin is a distinctive biopolymer composed of a poly-aspartate backbone adorned with arginine side chains, produced by cyanobacteria and certain bacterial strains through the enzymatic activities of CphA1 and CphA2. The CphA1 enzyme engages aspartate and arginine in separate reactions, while CphA2 facilitates a more streamlined polymerization of β-Asp-Arg dipeptides, potentially enhancing its efficiency for biotechnological applications. Although cyanophycin is typically insoluble at neutral pH, it becomes soluble in highly acidic or alkaline environments, leading to the formation of large, inert granules that play essential biological roles. This biopolymer primarily acts as a storage reservoir for nitrogen, carbon, and energy, with its metabolic processes tightly regulated to enable organisms to adapt to fluctuating environmental conditions. Cyanophycin’s versatility spans multiple sectors, including biomedicine, where it shows promise as a biocompatible material for drug delivery systems and tissue engineering scaffolds. In industrial contexts, it is being investigated as a biodegradable substitute for synthetic polymers and utilized in water treatment applications due to its high viscosity. In agriculture, cyanophycin-derived dipeptides are considered potential nutritional supplements because of their excellent bioavailability. Furthermore, recent advancements in the heterologous expression of cyanophycin synthetases in various host organisms, including bacterial hosts such as E. coli, yeasts, and plants, aim to improve production yields and create hybrid materials with optimized properties. Collectively, the multifunctionality and biodegradability of cyanophycin position it as a strong candidate for diverse applications, underscoring the necessity for continued research and development to enhance its practical use and commercial feasibility. This mini-review article summarizes the cyanophycin potential sources, chemical modifications, and potential applications.

HIGHLIGHTS

• Cyanophycin is a biopolymer of a poly-aspartate with arginine side chains.
• Cyanophycin is synthesized by the enzyme cyanophycin synthetase (CphA).
• Cyanophycin is extracted from cyanobacteria and is heterologously produced in bacteria, yeasts, and plants.
• Cyanophycin has a wide range of industrial, biomedical, and cosmeceutical applications.