Here we present data on the kinetics of insertion of melittin, a peptide from bee venom, into lipid membranes of different composition. Another component of bee venom is the enzyme phospholipase A2 (PLA2). We have examined the interaction of melittin and PLA2 with liposomes both separately and combined and demonstrate that they work synergistically to disrupt the membranes. A dramatic difference in the action of melittin and PLA2 is observed when the composition of the membrane is altered. Temperature also has a large effect on the kinetics of insertion and membrane disruption. We use a combination of techniques to measure liposome size (dynamic light scattering), peptide secondary structure (circular dichroism spectroscopy), peptide orient...
© 2010 Zubaidah NingsihA deeper understanding about the lipid-peptide interactions contributes sign...
AbstractWe have investigated the dependence of the lytic activity of the bee venom peptide melittin ...
The mechanism of interaction between a model antimicrobial peptide and phospholipid unilamellar vesi...
Here we present data on the kinetics of insertion of melittin, a peptide from bee venom, into lipid ...
Here we present data on the kinetics of insertion of melittin, a peptide from bee venom, into lipid ...
AbstractWe have examined the kinetics of the adsorption of melittin, a secondary amphipathic peptide...
AbstractMelittin, the soluble peptide of bee venom, has been demonstrated to induce lysis of phospho...
AbstractWe have examined the kinetics of the adsorption of melittin, a secondary amphipathic peptide...
Phospholipase A2 activation by membrane‐bound peptides was investigated in order to understand the r...
AbstractWe have investigated the dependence of the lytic activity of the bee venom peptide melittin ...
Lipid membranes act as catalysts for protein folding. Both alpha-helical and beta-sheet structures c...
AbstractThe peptide melittin, a 26 amino acid, cationic peptide from honey bee (Apis mellifera) veno...
Melittin, a bee venom, is a basic amphiphilic peptide, which mainly acts on the lipid matrix of memb...
© 2015 Dr. Andrew Cyrus RapsonThe development of antimicrobial resistance, which is the ability of m...
The mechanism of pore formation of lytic peptides, such as melittin from bee venom, is thought to in...
© 2010 Zubaidah NingsihA deeper understanding about the lipid-peptide interactions contributes sign...
AbstractWe have investigated the dependence of the lytic activity of the bee venom peptide melittin ...
The mechanism of interaction between a model antimicrobial peptide and phospholipid unilamellar vesi...
Here we present data on the kinetics of insertion of melittin, a peptide from bee venom, into lipid ...
Here we present data on the kinetics of insertion of melittin, a peptide from bee venom, into lipid ...
AbstractWe have examined the kinetics of the adsorption of melittin, a secondary amphipathic peptide...
AbstractMelittin, the soluble peptide of bee venom, has been demonstrated to induce lysis of phospho...
AbstractWe have examined the kinetics of the adsorption of melittin, a secondary amphipathic peptide...
Phospholipase A2 activation by membrane‐bound peptides was investigated in order to understand the r...
AbstractWe have investigated the dependence of the lytic activity of the bee venom peptide melittin ...
Lipid membranes act as catalysts for protein folding. Both alpha-helical and beta-sheet structures c...
AbstractThe peptide melittin, a 26 amino acid, cationic peptide from honey bee (Apis mellifera) veno...
Melittin, a bee venom, is a basic amphiphilic peptide, which mainly acts on the lipid matrix of memb...
© 2015 Dr. Andrew Cyrus RapsonThe development of antimicrobial resistance, which is the ability of m...
The mechanism of pore formation of lytic peptides, such as melittin from bee venom, is thought to in...
© 2010 Zubaidah NingsihA deeper understanding about the lipid-peptide interactions contributes sign...
AbstractWe have investigated the dependence of the lytic activity of the bee venom peptide melittin ...
The mechanism of interaction between a model antimicrobial peptide and phospholipid unilamellar vesi...