Photolytic control of peptide self-assembly.
Herein, we present a methodology that allows for the temporal control of fibrillization of amyloidogenic peptides. This general approach implements a photolabile linker that connects the amyloidogenic peptide to a fibril-inhibitory unit, in this case, a pentamer of amino acids modified with the solubilizing N,N-dimethylethylenediamine (DMDA) units. Upon photolysis, the linker can be dissociated to afford the intact and native amyloidogenic peptide. This methodology should be of value in a variety of studies where spatial and temporal control of supramolecular association processes is desired.
Bosques
Carlos J
CJ
Departments of Chemistry and Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Imperiali
Barbara
B
D000595:Amino Acid Sequence; D000682:Amyloid / Q000138:chemical synthesis / Q000737:chemistry*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009596:Nitrophenols; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D010782:Photolysis; D011422:Propionates / Q000737:chemistry
C107988:3-amino-3-(2-nitrophenyl)propionic acid; D000682:Amyloid; D009596:Nitrophenols; D010455:Peptides; D011422:Propionates