<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Alnajjar MA</submitter><funding>Deutsche Forschungsgemeinschaft</funding><pagination>e17709</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12851007</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>65(5)</volume><pubmed_abstract>Membrane-active peptides (MAPs) are a major class of peptides that renders lipid bilayer membranes permeable for hydrophilic compounds. MAPs include cell-penetrating peptides (CPPs) and pore-forming antimicrobial peptides (AMPs), which are believed to be mechanistically related. CPPs render the membrane sufficiently permeable to enable their own translocation, while AMPs create membrane damage and induce cell death. We report herein a fluorescence-based, dual-channel assay, which combines a classical dye efflux assay based on self-quenched carboxyfluorescein (CF) and a recently established supramolecular tandem membrane assay based on the supramolecular host-dye complex of p-sulfonatocalix[4]arene (CX4) and lucigenin (LCG). The new assay provides a functional classification of MAPs, which </pubmed_abstract><journal>Angewandte Chemie (International ed. in English)</journal><pubmed_title>Dual-Channel Fluorescence Assays with Supramolecular Host-Dye Reporter Pairs for Membrane Activity Mapping of Peptides.</pubmed_title><pmcid>PMC12851007</pmcid><funding_grant_id>467446229</funding_grant_id><pubmed_authors>Muller L</pubmed_authors><pubmed_authors>Nau WM</pubmed_authors><pubmed_authors>Hennig A</pubmed_authors><pubmed_authors>Reingolz T</pubmed_authors><pubmed_authors>Neumann J</pubmed_authors><pubmed_authors>Nilam M</pubmed_authors><pubmed_authors>Alnajjar MA</pubmed_authors><pubmed_authors>Pramod M</pubmed_authors><pubmed_authors>Schopper SN</pubmed_authors></additional><is_claimable>false</is_claimable><name>Dual-Channel Fluorescence Assays with Supramolecular Host-Dye Reporter Pairs for Membrane Activity Mapping of Peptides.</name><description>Membrane-active peptides (MAPs) are a major class of peptides that renders lipid bilayer membranes permeable for hydrophilic compounds. MAPs include cell-penetrating peptides (CPPs) and pore-forming antimicrobial peptides (AMPs), which are believed to be mechanistically related. CPPs render the membrane sufficiently permeable to enable their own translocation, while AMPs create membrane damage and induce cell death. We report herein a fluorescence-based, dual-channel assay, which combines a classical dye efflux assay based on self-quenched carboxyfluorescein (CF) and a recently established supramolecular tandem membrane assay based on the supramolecular host-dye complex of p-sulfonatocalix[4]arene (CX4) and lucigenin (LCG). The new assay provides a functional classification of MAPs, which </description><dates><release>2026-01-01T00:00:00Z</release><publication>2026 Jan</publication><modification>2026-06-14T06:05:02.628Z</modification><creation>2026-06-14T03:16:54.974Z</creation></dates><accession>S-EPMC12851007</accession><cross_references><pubmed>41388792</pubmed><doi>10.1002/anie.202517709</doi></cross_references></HashMap>