Enhanced Membrane Pore Formation by Multimeric/Oligomeric Antimicrobial Peptides
| Autor: | Arnusch, Christopher J., Branderhorst, Hilbert, De Kruijff, Ben, Liskamp, Rob M. J., Breukink, Eefjan, Pieters, Roland J., Dep Farmaceutische wetenschappen, Dep Scheikunde, Aandachtsgebieden, Medicinal Chemistry, Chemical Biology 1, Afd Chemical Biology and Drug Discovery |
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| Přispěvatelé: | Dep Farmaceutische wetenschappen, Dep Scheikunde, Aandachtsgebieden, Medicinal Chemistry, Chemical Biology 1, Afd Chemical Biology and Drug Discovery |
| Rok vydání: | 2007 |
| Předmět: |
Cell Membrane Permeability
in vitro study channel gating Antimicrobial peptides chemistry.chemical_element Magainins Models Biological Biochemistry Divalent chemistry.chemical_compound Organic chemistry Unilamellar Liposomes cycloaddition polypeptide antibiotic agent chemistry.chemical_classification Vesicle article Magainin Phosphatidylglycerols Fluoresceins Copper Cycloaddition In vitro Membrane priority journal chemistry copper ion Phosphatidylcholines Biophysics Antimicrobial Cationic Peptides |
| Zdroj: | Biochemistry, 46(46), 13437. American Chemical Society : Division of Carbohydrate Chemistry |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | The pore-forming antibacterial peptide magainin 2 was made divalent, tetravalent, and octavalent via a copper(I)-mediated 1-3 dipolar cycloaddition reaction ("click" chemistry). This series of pore-forming compounds was tested in vitro for their ability to form pores in large unilamillar vesicles (LUVs). A large increase in the pore-forming capability was especially observed with the tetravalent and octavalent magainin compounds in the LUVs consisting of DOPC, and the octavalent magainin compound showed a marked increase with the DOPC/DOPG LUVs. Activity was observed in the low nanomolar range for these compounds. © 2007 American Chemical Society. |
| Databáze: | OpenAIRE |
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