Abstract Non-ionic detergents enable the investigation of cell membranes, including biomolecule purification and drug delivery.The question of whether non-ionic detergents associated with satisfying protein yields following extraction and affinity purification of proteins from lysed E.coli membranes can amplify antibiotics on whole-cell E.
coli remains chervo jacke herren to be addressed.We unlock the modular chemistry of linear triglycerol detergents to reveal that more polar, non-ionic detergents that form globular micelles work better in amplifying antimicrobial activities of antibiotics than in purifying the membrane proteins mechanosensitive channel and aquaporin Z.Less polar detergents that form worm-like micelles indicate poor performances in both applications.
With chromatography we demonstrate how fine-tuning the polarity of chemical linkers between detergent headgroups and tails can sten jacket m switch the utility of detergents from protein purification to antibiotic amplification.We anticipate our findings to be a starting point for structure-property studies to better understand detergent designs in supramolecular chemistry and membrane research.