PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 35622592-2 2022 Rather than interacting with a specific receptor, melittin interacts with the lipid components, disrupting the lipid bilayer and inducing ion leakage and osmotic shock. Lipid Bilayers 111-124 melittin Apis mellifera 50-58 1314707-9 1992 We conclude that melittin-induced rigidization of the lipid bilayer may induce a reorganization of lipid assemblies as well as the rearrangements in membrane protein pattern and consequently the alterations in lipid-protein interactions. Lipid Bilayers 54-67 melittin Apis mellifera 17-25 3427031-4 1987 This paper describes the synthesis of the major form of melittin, using stepwise solid-phase methodology and the demonstration that the synthetic melittin, devoid of the minor component (N-formylmelittin) and other contaminants, interacts with lipid bilayers to form channels which are qualitatively indistinguishable from the ones formed by the naturally occurring toxin. Lipid Bilayers 244-258 melittin Apis mellifera 56-64 3427031-4 1987 This paper describes the synthesis of the major form of melittin, using stepwise solid-phase methodology and the demonstration that the synthetic melittin, devoid of the minor component (N-formylmelittin) and other contaminants, interacts with lipid bilayers to form channels which are qualitatively indistinguishable from the ones formed by the naturally occurring toxin. Lipid Bilayers 244-258 melittin Apis mellifera 146-154 35001445-3 2022 Recent advances have led to the development of two newer melittin analogues, MelP5 and Macrolittin 70, with improved pore formation in lipid bilayers while possessing fewer positive charges relative to natural melittin. Lipid Bilayers 135-149 melittin Apis mellifera 57-65 26074009-1 2015 The peptide melittin, a 26 amino acid, cationic peptide from honey bee (Apis mellifera) venom, disrupts lipid bilayer membranes in a concentration-dependent manner. Lipid Bilayers 104-117 melittin Apis mellifera 12-20