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Antimicrobial and Hemolytic Activity of Stapled Heptapeptide Dimers
Author(s) -
Luong Huy X.,
Kim DoHee,
Lee BongJin,
Kim YoungWoo
Publication year - 2016
Publication title -
bulletin of the korean chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.237
H-Index - 59
ISSN - 1229-5949
DOI - 10.1002/bkcs.10839
Subject(s) - antimicrobial , linker , chemistry , amphiphile , stereochemistry , antibiotics , antibiotic resistance , structure–activity relationship , biochemistry , combinatorial chemistry , in vitro , organic chemistry , operating system , polymer , computer science , copolymer
To improve the antimicrobial activity of the hydrocarbon‐stapled amphipathic heptapeptide helix identified from our previous study, we prepared a series of its dimeric analogs using several different linkers. All of these dimers showed a significant increase in antimicrobial activity although their hemolytic activity was also largely increased. One particular analog bearing a proline linker displayed notably low hemolytic activity compared to others, indicating that the conformational characteristics of the linker play a key role in disassociating undesirable hemolytic activity from antimicrobial activity in this series of antimicrobial peptides. We believe that this analog can serve as a stepping stone for further development of novel antimicrobial agents to combat antibiotic‐resistance.