Results 11 to 20 of about 15,825 (230)

Dual-Channel Fluorescence Assays with Supramolecular Host-Dye Reporter Pairs for Membrane Activity Mapping of Peptides. [PDF]

Angew Chem Int Ed Engl
Membrane‐active peptides (MAPs) such as cell‐penetrating peptides (CPPs) and antimicrobial peptides (AMPs) can translocate across lipid membranes and create membrane pores. The combination of a dye efflux and a supramolecular tandem membrane assay in a dual‐channel format enables an advanced mechanistic characterization and an exploration of the ...
Alnajjar MA, Schöpper SN, Pramod M, Reingolz T, Müller L, Neumann J, Nilam M, Nau WM, Hennig A.   +8 more
europepmc   +2 more sources

A new therapeutic approach for bone metastasis in colorectal cancer: intratumoral melittin

Journal of Venomous Animals and Toxins including Tropical Diseases, 2022
Background: Melittin has shown antiproliferative effects on tumor cells. Therefore, it comprises a valuable compound for studies on cancer treatment. To the best of our knowledge, no studies have reported melittin effects on bone metastasis.
Mackson Martins Rocha, Isabela Dariva, Gabriela Comelli Zornoff, Giovanna Sanches De Laurentis, Giulia Carli Mendes, Maycon Giovani Santana, Guilherme Chohfi de Miguel, Rui Seabra Ferreira Junior, Juliana Mozer Sciani, Denise Gonçalves Priolli   +9 more
doaj   +1 more source

Designing of RNA Molecule Translating for Activitable Melit-tin as Selective Targeting of Leishmania Infected Cells

Iranian Journal of Parasitology, 2021
Background: Leishmaniasis is characterized by strong inflammatory responses with high levels of inflammatory cytokines that induce microRNA 21 and matrix metalloproteinases.
Soheila Akhzari, Sedigheh Nabian, Parviz Shayan, Ramin Mazaheri Nezhad Fard, Minoo Soltani, Mohammad Taheri   +5 more
doaj   +1 more source

Free energy barrier for melittin reorientation from a membrane-bound state to a transmembrane state [PDF]

, 2013
An important step in a phospholipid membrane pore formation by melittin antimicrobial peptide is a reorientation of the peptide from a surface into a transmembrane conformation.
Allende D., Almeida P. F., Andersson M., Berneche S., Chen F. Y., Constantinescu I., de Jongh H. H. J., Glattli A., Gordon-Grossman M., Hess B., Hristova K., Huang H. W., Huang H. W., Humphrey W., Irudayam S. J., Irudayam S. J., Jämbeck J. P. M., Klocek G., Kuchinka E., Ladokhin A. S., Lam K. L. H., Lin J. H., Lu N. Y., Manna M., Matsuzaki K., Max L. Berkowitz, Mihajlovic M., Mihajlovic M., Mihajlovic M., Naito A., Nguyen L. T., Pott T., Pott T., Qiu W. H., Raghuraman H., Raghuraman H., Raghuraman H., Raghuraman H., Santo K. P., Sengupta D., Sheeba J. Irudayam, Tobias Pobandt, Torrie G. M., Ulmschneider J. P., Vivcharuk V., Wessman P., Wiedman G., Wimley W. C., Wimley W. C., Yang L., Yeh I. C.   +50 more
core   +3 more sources

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

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, AA Strömstedt, B Alberts, Christoph Gerber, CV Robinson, E Rakhmatullina, E Reimhult, FM Battiston, G Binnig, G Schwarz, GM Whitesides, H Raghuraman, Hans-Peter Lang, I Pera, J Fritz, J Mertens, J Popplewell, J Zhang, JE Sader, KM Hansen, M Mally, M Watari, Martin Hegner, MK Ghatkesar, MK Ghatkesar, Murali Krishna Ghatkesar, MW Kirschner, N Backmann, R Maget-Dana, S Dohn, S Rex, Sotirios Koutsopoulos, T Braun, T Braun, T Braun, T Braun, T Cha, Thomas Braun, TP Burg, Y Deng, Z Bálint   +40 more
core   +5 more sources

Melittin restores PTEN expression by down-regulating HDAC2 in human hepatocelluar carcinoma HepG2 cells.

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, Bin Zhao, Cheng Huang, Xiao-Ming Meng, Er-Bao Bian, Jun Li   +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, Grondelle, R. van, Kraayenhof, R., Larsen, O.F.A., Pandit, A., Stokkum, I.H.M. van   +5 more
core   +5 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, Fiore, Alberto, Guidelli, Rolando, Scaloni, Andrea, Toppi, Arianna   +4 more
core   +2 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 , Zeynep KALAYCIOĞLU, Sevgi KOLAYLI, Bedia BERKER   +3 more
doaj   +1 more source