Helicity-directed recognition of bacterial phospholipid via radially amphiphilic antimicrobial peptides.

ABSTRACT: The fundamental differences in phospholipids between bacterial and mammalian cell membranes present remarkable opportunities for antimicrobial design. However, it is challenging to distinguish bacterial anionic phospholipid phosphatidylglycerol (PG) from mammalian anionic phosphatidylserine (PS) with the same net charge. Here, we report a class of radially amphiphilic α helix antimicrobial peptides (RAPs) that can selectively discriminate PG from PS, relying on the helix structure. The representative RAP, L₁₀-MMBen, can direct the rearrangement of PG vesicles into a lamellar structure with its helix axis parallel to the PG membrane surface. The helical structure imparts both the thermodynamic and kinetic advantages of L₁₀-MMBen/PG assembly, and the hiding of hydrophob

SUBMITTER: Liang Y 

PROVIDER: S-EPMC11364095 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature