Peptide-Mediated Membrane Transport of Macromolecular Cargo Driven by Membrane Asymmetry.

Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370536 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-6882 (Electronic) Linking ISSN: 00032700 NLM ISO Abbreviation: Anal Chem Subsets: MEDLINE

Original Publication: Washington, American Chemical Society.

Cysteamine/*analogs & derivatives ; Lipid Bilayers/*metabolism ; Lipids/*chemistry ; Peptides/*metabolism ; beta-Galactosidase/*metabolism; Cysteamine/chemistry ; Cysteamine/metabolism ; Lipid Bilayers/chemistry ; Macromolecular Substances/chemistry ; Macromolecular Substances/metabolism ; Particle Size ; Peptides/chemistry ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Surface Properties ; beta-Galactosidase/chemistry

Pep-1 is a cell-penetrating peptide that represents a powerful strategy for delivering large, hydrophilic therapeutic molecules into cells. Model membranes, such as lipid vesicles and planar bilayers, have been useful for investigating the direct translocation of cell-penetrating peptides. Here, we present a droplet interface bilayer-based approach to quantify pep-1-mediated β-galactosidase translocation. We found that β-galactosidase translocation is driven only by the negative transmembrane potential resulting from the asymmetric bilayers. The asymmetric droplet interface bilayer method may be generally applicable for high-throughput screening of the efficacy of cell-penetrating peptides.

0 (Lipid Bilayers)
0 (Lipids)
0 (Macromolecular Substances)
0 (Pep-1 peptide)
0 (Peptides)
0 (Recombinant Proteins)
5UX2SD1KE2 (Cysteamine)
EC 3.2.1.23 (beta-Galactosidase)

Date Created: 20171021 Date Completed: 20190408 Latest Revision: 20190408

20240829

10.1021/acs.analchem.7b03421

29050472