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 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.
Organic Chemistry Department, IMM Institute, Radboud University Nijmegen, Toernooiveld 1, 6525 ED, Nijmegen, The Netherlands. D.Lowik@science.ru.nl
Dennis W P M
DW
Löwik
Joris T
JT
Meijer
Inge J
IJ
Minten
Henri
H
van Kalkeren
Lisa
L
Heckenmüller
Ines
I
Schulten
Kwinten
K
Sliepen
Peter
P
Smittenaar
Jan C M
JC
van Hest
D002942:Circular Dichroism; D046529:Microscopy, Electron, Transmission; D015394:Molecular Structure; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*
D010455:Peptides