Results 21 to 30 of about 18,137 (273)
Breathing Life into Polycations [PDF]
, 2008 The lack of efficient delivery systems is still limiting the full therapeutic potential of siRNA. For the purpose of nucleic acid transfer, among other synthetic carrier systems, polycations have been applied.
Meyer, Martin +4 more
core +1 more source
Emulsion-Based Intradermal Delivery of Melittin in Rats
Molecules, 2017 Bee venom (BV) has long been used as a traditional medicine. The aim of the present study was to formulate a BV emulsion with good rheological properties for dermal application and investigate the effect of formulation on the permeation of melittin ...
Sang Mi Han, Se Gun Kim, Sok Cheon Pak
doaj +1 more source
PLoS ONE, 2014 Melittin is a water-soluble toxic peptide derived from the venom of the bee. Although many studies show the anti-tumor activity of melittin in human cancer including glioma cells, the underlying mechanisms remain elusive.
Hui Zhang +5 more
doaj +1 more source
Ultrafast polarized fluorescence measurements on monomeric and self-associated melittin [PDF]
, 2003 The anisotropic and magic-angle fluorescence decay of the single tryptophan (Trp) residue of melittin, a bee venom peptide, was investigated by time-resolved fluorescence anisotropy using a streak camera setup.
Amerongen, H. van +5 more
core +5 more sources
Comparative Determination of Melittin by Capillary Electrophoretic Methods
Journal of the Turkish Chemical Society, Section A: Chemistry, 2021 Bee venom from honey bees (Apis Mellifera L.) is known to have many pharmacological and biological properties. Melittin, a peptide consisting of 26 amino acids, is known as the main component of bee venom.
Melda AKAY +3 more
doaj +1 more source
Helical Structure of Recombinant Melittin [PDF]
The Journal of Physical Chemistry B, 2018 Melittin is an extensively studied, 26-residue toxic peptide from honey bee venom. Because of its versatility in adopting a variety of secondary (helix or coil) and quaternary (monomer or tetramer) structures in various environments, melittin has been the focus of numerous investigations as a model peptide in protein folding studies as well as in ...
Lisa S. Ramirez +2 more
openaire +2 more sources
Channel-forming activity of syringopeptin 25 A in mercury-supported phospholipid monolayers and negatively charged bilayers [PDF]
, 2016 Interactions of the cationic lipodepsipeptide syringopeptin 25 A (SP25A) with mercury-supported dioleoylphosphatidylcholine (DOPC), dioleoylphosphatidylserine (DOPS) and dioeleoylphosphatidic acid (DOPA) self-assembled monolayers (SAMs) were investigated
Becucci, Lucia +4 more
core +2 more sources
Conformational changes in melittin upon complexation with an anionic melittin analog
FEBS Letters, 1991 Melittin and its Glu‐(7,21,22,23,24) analog upon mixing in equimolar concentrations form a hybrid oligomer with significant helical structure, in conditions in which each peptide separately adopts a largely disordered structure. The hybrid exhibits both cold‐ and heat‐induced denaturations similar to the phenomena exhibited by proteins. The hybrid also
Ramalingam, Kalaiyarasi +2 more
openaire +2 more sources
Melittin‐induced fusion of acidic liposomes [PDF]
FEBS Letters, 1983 Melittin‐induced fusion of acidic liposomes. Fusion was observed in the electron‐microscope and assayed as intermixing of both liposomes' contents and membranes. The melittin concentrations required for fusion induction were in the μM range compared to over 10 mM Ca2+ required for a comparable effect.
Eytan, Gera D., Almary, Taiser
openaire +2 more sources
Comprehensive characterization of molecular interactions based on nanomechanics [PDF]
, 2008 Molecular interaction is a key concept in our understanding of the biological mechanisms of life. Two physical properties change when one molecular partner binds to another.
A Bietsch +40 more
core +5 more sources