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Oligopeptide Helical Conformations Control Gold Nanoparticle Cross‐Linking
Author(s) -
Lyu Yanchao,
Marafon Giulia,
Martínez Álvaro,
Moretto Alessandro,
Scrimin Paolo
Publication year - 2019
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201902552
Subject(s) - random coil , surface plasmon resonance , peptide , folding (dsp implementation) , dynamic light scattering , chemistry , nanoparticle , colloidal gold , biophysics , circular dichroism , crystallography , materials science , nanotechnology , biochemistry , biology , engineering , electrical engineering
Peptide sequences functionalized with primary amines at the N‐ and C‐terminus are able to induce the aggregation of gold nanoparticles in ethanol as a consequence of their folding into a helical conformation. Random coil peptides are unable to induce such an aggregation process. Aggregation can be monitored spectrophotometrically by following the shift of the surface plasmon resonance (SPR) band of the nanoparticles and is confirmed by transmission electron microscopy and dynamic light scattering analyses. Partial denaturation of the peptides results in diminished cross‐linking ability. The helicity parameter θ 222 / θ 208 correlates fairly well with the shift of the SPR band to longer wavelengths, supporting the relationship between the amount of helical content of a peptide sequence and its ability to induce aggregation.