| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1249543 | Vibrational Spectroscopy | 2016 | 6 Pages |
Abstract
In this study, we present adsorption geometry of the mutated C-terminal analogue of neuropeptide Y (NPY), acetyl-[Leu28,31]-NPY(24-36), immobilized onto different SERS-active substrates (colloidal and specifically prepared in oxidation-reduction cycles Ag and Au substrates). Some changes in the adsorption geometry of the investigated peptide immobilized onto these SERS-active substrates are observed. The obtained SERS results demonstrated that the Tyr and Arg residues are mainly responsible for the molecule/metal interaction onto the Ag and Au surfaces.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Helena Domin, Dominika Święch, Natalia Piergies, Ewa Pięta, Younkyoo Kim, Edyta Proniewicz,
![First Page Preview: Characterization of the surface geometry of acetyl-[Leu28,31]-NPY(24-36), a selective Y2 receptor agonist, onto the Ag and Au surfaces Characterization of the surface geometry of acetyl-[Leu28,31]-NPY(24-36), a selective Y2 receptor agonist, onto the Ag and Au surfaces](/preview/png/1249543.png)