Adsorption of neurotensin-family peptides on SERS-active Ag substrates

2012
journal article
article
8
cris.lastimport.wos2024-04-10T01:30:49Z
dc.abstract.enKinetensin (KN) and its amino acids 1-8 fragment ([des-Leu$^{9}$]KN), neuromedin N (NMN), and xenopsin (XP) and its two analogs (XP-1 and XP-2) belong to the neurotensin family of peptides and are known to stimulate the growth of human tumors. In this work, we report Fourier transform-Raman and surface-enhanced Raman scattering (SERS) studies of these peptides and discuss their structures, orientation, and mode of adsorption onto a highly specific, electrochemically roughened SERS-active Ag electrode that is characterized by the formation of a 50-150nm Ag island on its surface. We show that the investigated peptides bind preferentially to this surface by substantial electronic overlap between the metal surface and the $\pi$-orbitals of the benzene rings of the Phe, Tyr, and Trp residues, which forces them to take parallel or almost parallel orientations with respect to the surface. In addition, the -$CH_{2}$-,-$CNH_{2}$, and -COO$^{-}$ molecular fragments are involved in interactions with (binding to or in close proximity with) the Ag surface. The SERS data show that the adsorption modes in each of these cases are very similar. In addition, we show that the specific differences in the amino acid sequences do not significantly affect the orientation of the investigated peptides on the Ag substrate. This result implies that the N -termini of the neurotensin-family peptides do not influence the mode for adsorption onto the Ag substrates.pl
dc.affiliationWydział Chemii : Zakład Fizyki Chemicznejpl
dc.contributor.authorProniewicz, Edyta - 131481 pl
dc.contributor.authorKudelski, Andrzejpl
dc.contributor.authorKim, Younkyoopl
dc.contributor.authorProniewicz, Leonard - 131552 pl
dc.date.accessioned2015-08-31T11:59:06Z
dc.date.available2015-08-31T11:59:06Z
dc.date.issued2012pl
dc.description.additionalNa publikacji autorka Proniewicz Edyta podpisana jako Podstawka‐Proniewicz Edyta.pl
dc.description.admin[AU]Proniewicz, Edyta [SAP11017634]pl
dc.description.number9pl
dc.description.physical1196-1203pl
dc.description.points35pl
dc.description.volume43pl
dc.identifier.doi10.1002/jrs.4034pl
dc.identifier.eissn1097-4555pl
dc.identifier.issn0377-0486pl
dc.identifier.urihttp://ruj.uj.edu.pl/xmlui/handle/item/15170
dc.languageengpl
dc.language.containerengpl
dc.rightsDodaję tylko opis bibliograficzny*
dc.rights.licencebez licencji
dc.rights.uri*
dc.subject.ensurface-enhanced Raman scatterinpl
dc.subject.enkinetensinpl
dc.subject.enneurotensin-family peptidespl
dc.subject.enneuromedin Npl
dc.subject.enxenopsinpl
dc.subtypeArticlepl
dc.titleAdsorption of neurotensin-family peptides on SERS-active Ag substratespl
dc.title.journalJournal of Raman Spectroscopypl
dc.typeJournalArticlepl
dspace.entity.typePublication
cris.lastimport.wos
2024-04-10T01:30:49Z
dc.abstract.enpl
Kinetensin (KN) and its amino acids 1-8 fragment ([des-Leu$^{9}$]KN), neuromedin N (NMN), and xenopsin (XP) and its two analogs (XP-1 and XP-2) belong to the neurotensin family of peptides and are known to stimulate the growth of human tumors. In this work, we report Fourier transform-Raman and surface-enhanced Raman scattering (SERS) studies of these peptides and discuss their structures, orientation, and mode of adsorption onto a highly specific, electrochemically roughened SERS-active Ag electrode that is characterized by the formation of a 50-150nm Ag island on its surface. We show that the investigated peptides bind preferentially to this surface by substantial electronic overlap between the metal surface and the $\pi$-orbitals of the benzene rings of the Phe, Tyr, and Trp residues, which forces them to take parallel or almost parallel orientations with respect to the surface. In addition, the -$CH_{2}$-,-$CNH_{2}$, and -COO$^{-}$ molecular fragments are involved in interactions with (binding to or in close proximity with) the Ag surface. The SERS data show that the adsorption modes in each of these cases are very similar. In addition, we show that the specific differences in the amino acid sequences do not significantly affect the orientation of the investigated peptides on the Ag substrate. This result implies that the N -termini of the neurotensin-family peptides do not influence the mode for adsorption onto the Ag substrates.
dc.affiliationpl
Wydział Chemii : Zakład Fizyki Chemicznej
dc.contributor.authorpl
Proniewicz, Edyta - 131481
dc.contributor.authorpl
Kudelski, Andrzej
dc.contributor.authorpl
Kim, Younkyoo
dc.contributor.authorpl
Proniewicz, Leonard - 131552
dc.date.accessioned
2015-08-31T11:59:06Z
dc.date.available
2015-08-31T11:59:06Z
dc.date.issuedpl
2012
dc.description.additionalpl
Na publikacji autorka Proniewicz Edyta podpisana jako Podstawka‐Proniewicz Edyta.
dc.description.adminpl
[AU]Proniewicz, Edyta [SAP11017634]
dc.description.numberpl
9
dc.description.physicalpl
1196-1203
dc.description.pointspl
35
dc.description.volumepl
43
dc.identifier.doipl
10.1002/jrs.4034
dc.identifier.eissnpl
1097-4555
dc.identifier.issnpl
0377-0486
dc.identifier.uri
http://ruj.uj.edu.pl/xmlui/handle/item/15170
dc.languagepl
eng
dc.language.containerpl
eng
dc.rights*
Dodaję tylko opis bibliograficzny
dc.rights.licence
bez licencji
dc.rights.uri*
dc.subject.enpl
surface-enhanced Raman scatterin
dc.subject.enpl
kinetensin
dc.subject.enpl
neurotensin-family peptides
dc.subject.enpl
neuromedin N
dc.subject.enpl
xenopsin
dc.subtypepl
Article
dc.titlepl
Adsorption of neurotensin-family peptides on SERS-active Ag substrates
dc.title.journalpl
Journal of Raman Spectroscopy
dc.typepl
JournalArticle
dspace.entity.type
Publication

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