Generation of artificial channels by multimerization of β-strands from natural porin
-
Marco Lolicato
,
Roland Benz
Abstract
General diffusion porins are passive transmembrane channels. We have explored the possibility to create artificial nanopores starting from natural β-barrel structures. Structural elements of bacterial porins were used to build a series of artificial nanopores. The basic module was selected by multi-alignment of general diffusion porins. The sequence corresponded to a highly conserved motif containing two β-strands, which was obtained from Escherichia coli OmpF. Dimeric to octameric repeats were obtained through cDNA recombinant technology. The hexameric repeat was used to test its properties. This protein was expressed, purified and reconstituted in the planar bilayer membranes. It was able to form channels in membranes with a conductance of 300 pS in 150 mm KCl and did not show any relevant voltage-dependence.
©2011 by Walter de Gruyter Berlin Boston
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Artikel in diesem Heft
- GENES AND NUCLEIC ACIDS
- Sequence elements outside the catalytic core of natural hairpin ribozymes modulate the reactions differentially
- PROTEIN STRUCTURE AND FUNCTION
- Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins
- Novel neutrophil inhibitory factor homologue in the buccal gland secretion of Lampetra japonica
- MEMBRANES, LIPIDS, GLYCOBIOLOGY
- Generation of artificial channels by multimerization of β-strands from natural porin
- MOLECULAR MEDICINE
- Gender-related differences in the oxidant state of cells in Fanconi anemia heterozygotes
- CELL BIOLOGY AND SIGNALING
- Mesothelial cells activate the plasma kallikrein-kinin system during pleural inflammation
- Impact of aryl hydrocarbon receptor (AhR) knockdown on cell cycle progression in human HaCaT keratinocytes
- PROTEOLYSIS
- Morpholino knockdown of the ubiquitously expressed transmembrane serine protease TMPRSS4a in zebrafish embryos exhibits severe defects in organogenesis and cell adhesion
- NOVEL TECHNIQUES
- Isolation of dipeptidyl peptidase IV (DP 4) isoforms from porcine kidney by preparative isoelectric focusing to improve crystallization
