HOST DEFENSE TEMPORIN 1 PEPTIDES AND THEIR POTENTIAL AS ANTIVIRAL AGENTS antimicrobial activity on a large number of invading microorganisms. They represent the most ancient and fast-acting elements of the host’s innate defence system against microbial pathogens. Methods: In this scenario, AMPs have emerged as good candidates for the generation of new anti-infective agents. While the antibacterial activity has been deeply investigated, the notions available for antiviral activities are still underexplored. Furthermore, due to their chemical and biological instability only few AMPs are currently in clinical trials as antimicrobial agents. The amphibian temporins represent one of the largest families (more than 100 members) and are among the smallest-sized AMPs (10-16 amino acids) found in nature to date. Temporins are known to be active particularly against Gram-positive bacteria, with minimal inhibitory concentrations ranging from 2.5 μM to 20 μM. In details, we focused on Temporin 1 (TL1) analogues. Results: Those peptides have been modified in order to increase the peptide stability and antimicrobial activity. We then performed a structure-activity relationship study of these peptides with the aim to improve their antimicrobial efficacy without altering their nonhemolytic character. Conclusion: Among the peptides generated, several of them have shown higher in solution stability, low toxicity and a significant decrease of Herpes Simplex virus type 1 infectivity. Our results show novel possible applications of Temporin 1 peptides in the field of antivirals.

HOST DEFENSE TEMPORIN 1 PEPTIDES AND THEIR POTENTIAL AS ANTIVIRAL AGENTS / Palomba, Luciana; Merlino, Francesco; Zannella, Carla; Franci, Gianluigi; Galdiero, Stefania; Grieco, Paolo; Galdiero, Massimiliano. - (2017). (Intervento presentato al convegno IUMS2017: 15th International Congress of Bacteriology & Applied Microbiology tenutosi a Singapore nel 17-21 July 2017).

HOST DEFENSE TEMPORIN 1 PEPTIDES AND THEIR POTENTIAL AS ANTIVIRAL AGENTS

Francesco Merlino;Stefania Galdiero;Paolo Grieco;
2017

Abstract

HOST DEFENSE TEMPORIN 1 PEPTIDES AND THEIR POTENTIAL AS ANTIVIRAL AGENTS antimicrobial activity on a large number of invading microorganisms. They represent the most ancient and fast-acting elements of the host’s innate defence system against microbial pathogens. Methods: In this scenario, AMPs have emerged as good candidates for the generation of new anti-infective agents. While the antibacterial activity has been deeply investigated, the notions available for antiviral activities are still underexplored. Furthermore, due to their chemical and biological instability only few AMPs are currently in clinical trials as antimicrobial agents. The amphibian temporins represent one of the largest families (more than 100 members) and are among the smallest-sized AMPs (10-16 amino acids) found in nature to date. Temporins are known to be active particularly against Gram-positive bacteria, with minimal inhibitory concentrations ranging from 2.5 μM to 20 μM. In details, we focused on Temporin 1 (TL1) analogues. Results: Those peptides have been modified in order to increase the peptide stability and antimicrobial activity. We then performed a structure-activity relationship study of these peptides with the aim to improve their antimicrobial efficacy without altering their nonhemolytic character. Conclusion: Among the peptides generated, several of them have shown higher in solution stability, low toxicity and a significant decrease of Herpes Simplex virus type 1 infectivity. Our results show novel possible applications of Temporin 1 peptides in the field of antivirals.
2017
HOST DEFENSE TEMPORIN 1 PEPTIDES AND THEIR POTENTIAL AS ANTIVIRAL AGENTS / Palomba, Luciana; Merlino, Francesco; Zannella, Carla; Franci, Gianluigi; Galdiero, Stefania; Grieco, Paolo; Galdiero, Massimiliano. - (2017). (Intervento presentato al convegno IUMS2017: 15th International Congress of Bacteriology & Applied Microbiology tenutosi a Singapore nel 17-21 July 2017).
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/770015
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