| Autor: |
Bui Thi Phuong, Hai, Do Hai, Yen, Nguyen Huu, Viet, Luong The, Anh, Nguyen Hong, Minh, Luong Xuan, Huy |
| Zdroj: |
Medicinal Chemistry Research; May2024, Vol. 33 Issue 5, p735-739, 5p |
| Abstrakt: |
Antimicrobial peptides (AMPs) are naturally occurring molecules that play a vital role in the innate immune responses of various organisms. Additionally, artificial AMPs are also designed based on the common structure-activity relationships (SARs) found in natural ones. As part of our ongoing effort to explore the advantages of each source, this study focused on two representative helical AMPs: Mastoparan C (MPC) and BP52. While the former is derived from the venom of the European wasp Vespa crabro, the latter belongs to a group of artificially designed AMPs inspired by the structure of two natural peptides, Cecropin A and Melittin M. Our data suggests that BP52 exhibits similar antimicrobial activity to MPC but demonstrates significantly higher potency against the A427 cancer cells. Taken together with the shorter length and reduced toxicity to human red blood cells, BP52 exhibited greater potential in drug development compared to its counterpart MPC, thus highlighting the potential of rational design in developing short, potent and selective membrane-active peptides. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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