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J Colloid Interface Sci. 2007 Apr 15;308(2):356-63. Epub 2007 Jan 31.

Structural control of peptide-coated gold nanoparticle assemblies by the conformational transition of surface peptides.

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  • 1Department of Chemistry for Materials, Graduate School of Engineering, Mie University, 1577 Kurimanakayama-Cho, Tsu, Mie 514-8507, Japan. higuchi@chem.mie-u.ac.jp

Abstract

Gold nanoparticles having peptide chains on the surfaces have been prepared yb ring-opening polymerization of gamma-methyl L-glutamate N-carboxyanhydride with fixed amino groups on the nanoparticle surface as an initiator. The number of peptide chains on the surface was adjusted to ca. 2 molecules per gold nanoparticle by controlling the number of fixed amino groups on the surface. The peptide chains on the surface were partially saponified to obtain poly(gamma-methyl L-glutamate-co-L-glutamic acid) with 28 mol% of glutamic acid residues. The number-average molecular weight of the peptide was 73,000. We described structural control of the peptide-coated gold nanoparticle assembly by conformational transition of the surface peptides. In deionized water, the peptide chains on the nanoparticle took a random coil conformation, and the individual nanoparticles existed in dispersed globular species. On the other hand, the peptide chains on the nanoparticle took an alpha-helical conformation in trifluoroethanol. Under this condition, the alpha-helical peptide chains on distinct gold nanoparticles connected the nanoparticles to form a fibril assembly owing to the dipole-dipole interaction between the surface peptide chains. The morphology of the peptide-coated gold nanoparticle assembly could be controlled by the conformational transition of surface peptides, which was attended by solution composition changes.

PMID:
17270198
[PubMed - indexed for MEDLINE]
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