1065010-73-2Relevant academic research and scientific papers
Temporin-SHa and its analogs as potential candidates for the treatment of helicobacter pylori
Olleik, Hamza,Baydoun, Elias,Perrier, Josette,Hijazi, Akram,Raymond, Josette,Manzoni, Marine,Dupuis, Lucas,Pauleau, Ghislain,Goudard, Yvain,de La Villéon, Bruno,Goin, Géraldine,Sockeel, Philippe,Choudhary, Muhammad Iqbal,Di Pasquale, Eric,Nadeem-Ul-haque, Muhammad,Ali, Hunain,Khan, Arif Iftikhar,Shaheen, Farzana,Maresca, Marc
, (2019)
Helicobacter pylori is one of the most prevalent pathogens colonizing 50% of the world's population and causing gastritis and gastric cancer. Even with triple and quadruple antibiotic therapies, H. pylori shows increased prevalence of resistance to conventional antibiotics and treatment failure. Due to their pore-forming activity, antimicrobial peptides (AMP) are considered as a good alternative to conventional antibiotics, particularly in the case of resistant bacteria. In this study, temporin-SHa (a frog AMP) and its analogs obtained by Gly to Ala substitutions were tested against H. pylori. Results showed differences in the antibacterial activity and toxicity of the peptides in relation to the number and position of D-Ala substitution. Temporin-SHa and its analog NST1 were identified as the best molecules, both peptides being active on clinical resistant strains, killing 90–100% of bacteria in less than 1 h and showing low to no toxicity against human gastric cells and tissue. Importantly, the presence of gastric mucins did not prevent the antibacterial effect of temporin-SHa and NST1, NST1 being in addition resistant to pepsin. Taken together, our results demonstrated that temporin-SHa and its analog NST1 could be considered as potential candidates to treat H. pylori, particularly in the case of resistant strains.
Studies on the antileishmanial properties of the antimicrobial peptides temporin A, B and 1Sa
Chadbourne, Frances L.,Raleigh, Catriona,Ali, Hayder Z.,Denny, Paul W.,Cobb, Steven L.
experimental part, p. 751 - 755 (2012/06/15)
Given the paucity and toxicity of available drugs for leishmaniasis, coupled with the advent of drug resistance, the discovery of new therapies for this neglected tropical disease is recognised as being of the utmost urgency. As such antimicrobial peptides (AMPs) have been proposed as promising compounds against the causative Leishmania species, insect vector-borne protozoan parasites. Here the AMP temporins A, B and 1Sa have been synthesised and screened for activity against Leishmania mexicana insect stage promastigotes and mammalian stage amastigotes, a significant cause of human cutaneous disease. In contrast to previous studies with other species the activity of these AMPs against L. mexicana amastigotes was low. This suggests that amastigotes from different Leishmania species display varying susceptibility to peptides from the temporin family, perhaps indicating differences in their surface structure, the proposed target of these AMPs. In contrast, insect stage L. mexicana promastigotes were sensitive to two of the screened temporins which clearly demonstrates the importance of screening AMPs against both forms of the parasite.
