Controlled disassembly of peptide amphiphile fibres

In this paper, the introduction of both a methionine residue and a nitrobenzyl derivative as a labile linker between the peptide part and the hydrophobic alkyl chain of a peptide amphiphile are presented. These modifications are shown not to inhibit the formation of structured assemblies that analog...

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Vydáno v:Journal of peptide science Ročník 14; číslo 2; s. 127 - 133
Hlavní autoři: Löwik, Dennis W. P. M., Meijer, Joris T., Minten, Inge J., van Kalkeren, Henri, Heckenmüller, Lisa, Schulten, Ines, Sliepen, Kwinten, Smittenaar, Peter, van Hest, Jan C. M.
Médium: Journal Article
Jazyk:angličtina
Vydáno: Chichester, UK John Wiley & Sons, Ltd 01.02.2008
Témata:
caged peptides
Circular Dichroism
Microscopy, Electron, Transmission
Molecular Structure
nano‐fibres
peptide amphiphiles
Peptides - chemical synthesis
Peptides - chemistry
self‐assembly
switching assembly
ISSN:1075-2617, 1099-1387
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Shrnutí:In this paper, the introduction of both a methionine residue and a nitrobenzyl derivative as a labile linker between the peptide part and the hydrophobic alkyl chain of a peptide amphiphile are presented. These modifications are shown not to inhibit the formation of structured assemblies that analogous peptide amphiphiles lacking the linkers are able to form. Moreover, the introduction of either labile linker allows removal of the peptide amphiphile's stabilizing hydrophobic moieties to initiate a controlled disassembly of fibre aggregates. This is achieved by either treatment with CNBr or UV irradiation, respectively. These disassembly mechanisms could be the starting point for methodology that allows further manipulation of self‐assembled peptide amphiphile architectures. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.
Bibliografie:This article is part of the Special Issue of the Journal of Peptide Science entitled “Peptides in Nanotechnology”.
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ISSN:1075-2617
1099-1387
DOI:10.1002/psc.969