Results 61 to 70 of about 11,509 (217)
Pore formation and translocation of melittin
Biophysical Journal, 1997 Melittin, a bee venom, is a basic amphiphilic peptide, which mainly acts on the lipid matrix of membranes, lysing various cells. To elucidate the molecular mechanism, we investigated its interactions with phospholipid vesicles. The peptide formed a pore with a short lifetime in the membrane, as revealed by the release of an anionic fluorescent dye ...
Matsuzaki, K. +2 more
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Molecules, 2016 Renal fibrosis is the principal pathological process underlying the progression of chronic kidney disease that leads to end-stage renal disease. Melittin is a major component of bee venom, and it has anti-bacterial, anti-viral, and anti-inflammatory ...
Hyun-Jin An +4 more
doaj +1 more source
Responsive Materials, EarlyView.Peptide‐based antibacterial nanoplatforms, encompassing self‐assembled peptides and peptide‐engineered inorganic, polymeric, and lipid nanocarriers, are systematically reviewed. The article highlights design principles and stimuli‐responsive regulation for improving peptide stability, delivery efficiency, and antibacterial performance.
Peng Tan +8 more
wiley +1 more source
Environmental Toxicology, EarlyView.ABSTRACT Cadmium (Cd) is a persistent environmental heavy metal and a major public health concern because it persists in the body for long periods and gradually accumulates in vital organs, particularly the liver, kidneys, and brain. Chronic Cd exposure promotes the excessive production of reactive oxygen species (ROS), which ultimately leads to ...
Soumaya Ghodbane +8 more
wiley +1 more source
Nature of Melittin-Phospholipid Interaction
Biophysical Journal, 1982 Melittin, the major protein component of bee venom that possesses a strong hemolytic activity (1), is an amphipathic protein whose amino acid residues 1-20 are predominantly hydrophobic; residues 21-26 are hydrophilic. Determination of the molecular basis and specificity of the attractive forces involved in its interaction with membranes is essential ...
Georghiou, S. +2 more
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The effect of counterions on melittin aggregation [PDF]
Biochemical Journal, 1983 Melittin, a surface-active polypeptide from bee venom, has an overall hydrophobic N-terminus, with basic residues clustered at the C-terminus. In aqueous solution melittin exists as a mixture of monomer and tetramer, the monomer adopting a predominantly random-coil configuration, whereas the tetramer is rich in α-helix.
A S, Tatham, R C, Hider, A F, Drake
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Interaction of melittin with solid supported membranes
, 2000 The interaction of the membrane active peptide melittin with solid supported lipid bilayers has been scrutinized by means of impedance spectroscopy and scanning force microscopy. Highly flexible lipid bilayers anchored via a hydrophilic spacer terminated
Janshoff, Andreas +5 more
core +1 more source
Impact of Honeybee Venom Melittin on Cell Viability of Different Prostate Cancer Lineages
Креативная хирургия и онкология, 2022 Background. Melittin is a major constituent of honeybee venom and comprises a water-soluble surfactant peptide with cytolytic effects potentially applicable in anticancer therapy.
R. R. Khalikov +6 more
doaj +1 more source
MedComm, Volume 7, Issue 11, November 2026.This comprehensive review summarizes gastric cancer epidemiology, multifactorial risk factors (like infectious, dietary, genetic), pathogenesis such as precancerous evolution, molecular alterations, and a focus on the bidirectional interactions between gastric cancer cells and macrophages in the tumor microenvironment.
Yixuan Xin +6 more
wiley +1 more source
Acyl Carrier Protein Interacts With Melittin
, 1990 Acyl carrier protein (ACP) from Escherichia coli has been shown to form complexes with melittin, a cationic peptide from bee venom. ACP is a small (Mr 8847), acidic, Ca2+-binding protein, which possesses some characteristics resembling those of ...
Ernst-Fonberg, Mary L. +2 more
core +1 more source