Jung G, Redemann T, Kroll K, Meder S, Hirsch A, Boheim G (2003)
Publication Type: Journal article, Original article
Publication year: 2003
Original Authors: Jung G., Redemann T., Kroll K., Meder S., Hirsch A., Boheim G.
Publisher: Wiley-Blackwell
Book Volume: 9
Pages Range: 784-798
DOI: 10.1002/psc.525
N- and C-terminally modified with fullerene or lipopeptide alamethicin molecules were designed for the formation of template-free, self-assembling, voltage-dependent ion conducting channels. The automated solid phase synthesis of the alamethicin-F30 sequence was performed by in situ fluoride activation on 2-chlorotritylchloride-polystyrene resin and the conjugation with fullerenes-C and -C was carried out in solution. Voltage-dependent bilayer experiments revealed preferred channel sizes for C-terminal alamethicin F30-fullerene-C and -C conjugates and higher activity compared with native alamethicin, whereas N-terminally linked fullerene balls destabilize pore formation. C-terminal alamethicin F30-fullerene-C70 conjugates show pore states with remarkably long lifetimes of seconds. C-terminal lipopeptide conjugates of alamethicin were prepared by coupling via short peptide spacers with synthetic tripalmitoyl-S-glyceryl-cysteine, which represents the strong membrane anchoring N-terminus of bacterial lipoprotein. Alamethicin-lipopeptide conjugates exhibit high channel forming activities, whereby they self-assemble and adopt preferred pore states with extremely long lifetimes. The novel membrane modifying peptaibol constructs are valuable lead compounds for developments in sensorics related to transmembrane ion conductance. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.
APA:
Jung, G., Redemann, T., Kroll, K., Meder, S., Hirsch, A., & Boheim, G. (2003). Template-free self-assembling fullerene and lipopeptide conjugates of alamethicin form voltage-dependent ion channels of remarkable stability and activity. Journal of Peptide Science, 9, 784-798. https://doi.org/10.1002/psc.525
MLA:
Jung, Günther, et al. "Template-free self-assembling fullerene and lipopeptide conjugates of alamethicin form voltage-dependent ion channels of remarkable stability and activity." Journal of Peptide Science 9 (2003): 784-798.
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