Bibliographic Details
| Title: |
Chemical linkers switch triglycerol detergents from bacterial protein purification to mild antibiotic amplification. |
| Authors: |
Singh, Abhishek Kumar, Seewald, Marc, Schade, Boris, Zoister, Christian, Haag, Rainer, Urner, Leonhard Hagen |
| Source: |
Communications Chemistry; 3/8/2025, Vol. 8 Issue 1, p1-11, 11p |
| Subject Terms: |
ESCHERICHIA coli, BACTERIAL proteins, MEMBRANE proteins, SUPRAMOLECULAR chemistry, CHEMICAL biology, AQUAPORINS |
| 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 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 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. Non-ionic detergents enable the investigation of cell membranes, but structure-property studies often remain limited. Here, the authors report on the modular synthesis of linear and dendritic triglycerol detergents to decipher the correlation between membrane protein purification, antibiotic amplification, and micellar polarities. [ABSTRACT FROM AUTHOR] |
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| Database: |
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