Aqueous self-assembly of unsymmetric Peptide bolaamphiphiles into nanofibers with hydrophilic cores and surfaces.
Unsymmetric peptide bolaamphiphiles that incorporate (l-glutamyl)3glycine at one terminus and either tetraethylene glycol or aspartic acid at the other were found to form hydrogels at low wt %, presumably by self-assembling into nanofibers presenting (l-glutamyl)3glycine at their surfaces and burying the second headgroup at their cores. Transmission electron microscopy measurements on 1 wt % gels negatively stained with phosphotungstic acid and positively stained with uranyl acetate show one-dimensional objects with diameters of 5 nm and lengths in excess of 1 mum. Circular dichroism and solid-state FTIR spectra indicate the adoption of beta-sheet structure within the nanofibers.
Claussen
Randal C
RC
Department of Chemistry, Northwestern University, Evanston, Illinois 60208, USA. s-stup@northwestern.edu
Rabatic
Bryan M
BM
Stupp
Samuel I
SI
D000409:Alanine / Q000031:analogs & derivatives; D002942:Circular Dichroism; D005998:Glycine / Q000031:analogs & derivatives; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D045333:Nanotubes, Peptide / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties; D014867:Water / Q000737:chemistry*
D045333:Nanotubes, Peptide; D010455:Peptides; D014867:Water; D000409:Alanine; D005998:Glycine