Phe-MetNH_2 terminal bombesin subfamily peptides : potential induced changes in adsorption on Ag, Au, and Cu electrodes monitored by SERS
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dc.type
JournalArticle
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dc.description.physical
4189-4200
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dc.description.additional
Na publikacji autorka Proniewicz Edyta podpisana jako Podstawka‐Proniewicz Edyta.
pl
dc.abstract.en
Surface-enhanced Raman scattering, electro-
chemistry, and generalized two-dimensional correlation
analysis methods were used to characterize phyllolitorin and
a peptide derived from
Pseudophryne guntheri
(PG-L).
Phyllolitorin and PG-L were deposited onto Ag, Au, and Cu
electrode surfaces at different applied electrode potentials in an
aqueous solution at physiological pH, and the orientations and
adsorption mechanisms of peptides were determined based on
the enhancement, broadening, and shifts in the wavenumbers
of specific bands. On the basis of these analyses, specific
conclusions were drawn regarding the peptide geometry and changes in the geometry that occurred when the electrode type and
applied electrode potential were varied. The phyllolitorin and PG-L deposited onto the Ag, Au, and Cu electrode surfaces
showed bands that were due to the vibrations of moieties in contact with or in close proximity to the electrode surfaces and were
thus located on the same side of the polypeptide backbone. These moieties included the Phe and Trp rings, the sulfur atom of
Met, and the amide bond. Variations in the arrangement of these fragments were observed with changes in the metal surface and
the applied electrode potential.