Solid-state NMR structural studies of peptides immobilized on gold nanoparticles.
In this paper we describe solid-state NMR experiments that provide information on the structures of surface-immobilized peptides. The peptides are covalently bound to alkanethiolates that are self-assembled as monolayers on colloidal gold nanoparticles. The secondary structure of the immobilized peptides was characterized by quantifying the Ramachandran angles phi and psi. These angles were determined in turn from distances between backbone carbonyl 13C spins, measured with the double-quantum filtered dipolar recoupling with a windowless sequence experiment, and by determination of the mutual orientation of chemical shift anisotropy tensors of 13C carbonyl spins on adjacent peptide planes, obtained from the double-quantum cross-polarization magic-angle spinning spectrum. It was found that peptides composed of periodic sequences of leucines and lysines were bound along the length of the peptide sequence and displayed a tight alpha-helical secondary structure on the gold nanoparticles. These results are compared to similar studies of peptides immobilized on hydrophobic surfaces.
Bower
P V
PV
Department of Chemistry, University of Washington, Seattle, Washington 98195-1700, USA.
Louie
E A
EA
Long
J R
JR
Stayton
P S
PS
Drobny
G P
GP
D005583:Fourier Analysis; D006046:Gold / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D049329:Nanostructures / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D008625:Tiopronin / Q000737:chemistry
D010455:Peptides; D006046:Gold; D008625:Tiopronin