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SYNTHESIS AND BIOLOGICAL COMPARISON OF TWO ANTIMICROBIAL PEPTIDES ORIGINATED FROM THE VENOM OF VESPA CRABRO AND POLYBIA PAULISTA
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Bee venom is abundant in potential antimicrobial peptides, AMPs, . Among them, Mastoparan C and Polybia-MP1 are two well-known AMPs that were found in the European Hornet Vespa crabro and social wasp Polybia paulista, respectively. Due to the potent antimicrobial activity toward a wide range of microbial pathogens, including Gram-negative, Gram-positive and fungal species, they are promising to tackle the global antimicrobial resistance crisis. Thus, understanding the structure and activity relationships (SARs) is essential for the development of potential therapeutic applications. In this study, we synthesized and compared the differences in biological properties of these two antimicrobial peptides. The preliminary data suggests various important information regarding the structural requirements for optimizing the pharmacological properties of antimicrobial peptides.
Publishing House for Science and Technology, Vietnam Academy of Science and Technology (Publications)
Title: SYNTHESIS AND BIOLOGICAL COMPARISON OF TWO ANTIMICROBIAL PEPTIDES ORIGINATED FROM THE VENOM OF VESPA CRABRO AND POLYBIA PAULISTA
Description:
Bee venom is abundant in potential antimicrobial peptides, AMPs, .
Among them, Mastoparan C and Polybia-MP1 are two well-known AMPs that were found in the European Hornet Vespa crabro and social wasp Polybia paulista, respectively.
Due to the potent antimicrobial activity toward a wide range of microbial pathogens, including Gram-negative, Gram-positive and fungal species, they are promising to tackle the global antimicrobial resistance crisis.
Thus, understanding the structure and activity relationships (SARs) is essential for the development of potential therapeutic applications.
In this study, we synthesized and compared the differences in biological properties of these two antimicrobial peptides.
The preliminary data suggests various important information regarding the structural requirements for optimizing the pharmacological properties of antimicrobial peptides.
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