Simple view
Full metadata view
Authors
Statistics
Influence of backbone length and synthetic mutations on orientation of neurotensin fragments adsorbed onto a colloidal silver surface : SERS studies
Journal
Journal of Raman Spectroscopy
Author
Proniewicz Leonard
Proniewicz Edyta
Pienpinijtham Prompong
Ozaki Yukihiro
Kim Younkyoo
Volume
44
Number
1
Pages
55-62
ISSN
0377-0486
eISSN
1097-4555
Language
English
Journal language
English
Abstract in English
Neurotensin (NT) is a naturally occurring neurotransmitter that mediates the metabotropic seven-transmembrane G protein- coupled receptors, namely NTR1s, richly expressed on tumor surface. Therefore, mutated active molecular fragments of NT that possess selective antagonist or weak agonist properties and the high af fi nity to NTR1 have attracted considerable interest for use in thrombus, in fl ammation, and imaging/treatment of tumors. In this work, SERS spectra of three N -terminal fragments of human NT (NT 1-6 ,NT 1-8 , and NT 1-11 ) and six speci fi cally mutated C -terminal fragments of human NT, including NT 8-13 , [Dab 9 ] NT 8-13 , [Lys 8 ,Lys 9 ]NT 8-13 , [Lys 8 -( W )-Lys 9 ]NT 8-13 , [Lys 9 ,Trp 11 ,Glu 12 ]NT 8-13 , and NT 9-13 , adsorbed onto nanometer-sized colloidal silver particles in an aqueous solution at pH level of the solution 2 are presented. A comparison was made between the struc- tures of the native and mutated fragments to determine how changes in peptide length and mutations of the structure in fl uenced the NT adsorption properties. Based on the interpretation of the obtained data, we showed that all of the investi- gated NT fragments, excluding [Lys 9 ,Trp 11 ,Glu 12 ]NT 8-13 , tended to adsorb on the silver surface mainly through the L-tyrosine residue and the carboxylate group. The Tyr ring lied more-or-less fl at on the silver surface. The hydrogen atom from the phenol group dissociated upon binding. On the other hand, [Lys 9 ,Trp 11 ,Glu 12 ]NT 8-13 bound to this substrate through the close to vertical co-pyrrole ring of the indole ring (Trp 11 ) and – COO
. Comparison of the presented data with those obtained earlier for NT allows to suggest that in the case of naturally occurring neurotensin, both Tyr residues together with the carboxylate group play crucial role in the binding to the nanome- ter-sized colloidal silver particles. This geometry of binding forces the NT molecule to lay fl at on the surface.
Affiliation
Wydział Chemii : Zakład Fizyki Chemicznej
Scopus© citations
5
dc.abstract.en | Neurotensin (NT) is a naturally occurring neurotransmitter that mediates the metabotropic seven-transmembrane G protein- coupled receptors, namely NTR1s, richly expressed on tumor surface. Therefore, mutated active molecular fragments of NT that possess selective antagonist or weak agonist properties and the high af fi nity to NTR1 have attracted considerable interest for use in thrombus, in fl ammation, and imaging/treatment of tumors. In this work, SERS spectra of three N -terminal fragments of human NT (NT 1-6 ,NT 1-8 , and NT 1-11 ) and six speci fi cally mutated C -terminal fragments of human NT, including NT 8-13 , [Dab 9 ] NT 8-13 , [Lys 8 ,Lys 9 ]NT 8-13 , [Lys 8 -( W )-Lys 9 ]NT 8-13 , [Lys 9 ,Trp 11 ,Glu 12 ]NT 8-13 , and NT 9-13 , adsorbed onto nanometer-sized colloidal silver particles in an aqueous solution at pH level of the solution 2 are presented. A comparison was made between the struc- tures of the native and mutated fragments to determine how changes in peptide length and mutations of the structure in fl uenced the NT adsorption properties. Based on the interpretation of the obtained data, we showed that all of the investi- gated NT fragments, excluding [Lys 9 ,Trp 11 ,Glu 12 ]NT 8-13 , tended to adsorb on the silver surface mainly through the L-tyrosine residue and the carboxylate group. The Tyr ring lied more-or-less fl at on the silver surface. The hydrogen atom from the phenol group dissociated upon binding. On the other hand, [Lys 9 ,Trp 11 ,Glu 12 ]NT 8-13 bound to this substrate through the close to vertical co-pyrrole ring of the indole ring (Trp 11 ) and – COO - . Comparison of the presented data with those obtained earlier for NT allows to suggest that in the case of naturally occurring neurotensin, both Tyr residues together with the carboxylate group play crucial role in the binding to the nanome- ter-sized colloidal silver particles. This geometry of binding forces the NT molecule to lay fl at on the surface. | pl |
dc.affiliation | Wydział Chemii : Zakład Fizyki Chemicznej | pl |
dc.contributor.author | Proniewicz, Leonard - 131552 | pl |
dc.contributor.author | Proniewicz, Edyta - 131481 | pl |
dc.contributor.author | Pienpinijtham, Prompong | pl |
dc.contributor.author | Ozaki, Yukihiro | pl |
dc.contributor.author | Kim, Younkyoo | pl |
dc.date.accessioned | 2015-06-24T07:23:22Z | |
dc.date.available | 2015-06-24T07:23:22Z | |
dc.date.issued | 2013 | pl |
dc.description.admin | [AB] Proniewicz, Edyta [SAP11017634] 50000141 | pl |
dc.description.number | 1 | pl |
dc.description.physical | 55-62 | pl |
dc.description.volume | 44 | pl |
dc.identifier.doi | 10.1002/jrs.4157 | pl |
dc.identifier.eissn | 1097-4555 | pl |
dc.identifier.issn | 0377-0486 | pl |
dc.identifier.uri | http://ruj.uj.edu.pl/xmlui/handle/item/10167 | |
dc.language | eng | pl |
dc.language.container | eng | pl |
dc.rights.licence | Bez licencji otwartego dostępu | |
dc.subtype | Article | pl |
dc.title | Influence of backbone length and synthetic mutations on orientation of neurotensin fragments adsorbed onto a colloidal silver surface : SERS studies | pl |
dc.title.journal | Journal of Raman Spectroscopy | pl |
dc.type | JournalArticle | pl |
dspace.entity.type | Publication |
dc.abstract.enpl
Neurotensin (NT) is a naturally occurring neurotransmitter that mediates the metabotropic seven-transmembrane G protein-
coupled receptors, namely NTR1s, richly expressed on tumor surface. Therefore, mutated active molecular fragments of NT
that possess selective antagonist or weak agonist properties and the high af
fi
nity to NTR1 have attracted considerable interest
for use in thrombus, in
fl
ammation, and imaging/treatment of tumors. In this work, SERS spectra of three
N
-terminal fragments
of human NT (NT
1-6
,NT
1-8
, and NT
1-11
) and six speci
fi
cally mutated
C
-terminal fragments of human NT, including NT
8-13
, [Dab
9
]
NT
8-13
, [Lys
8
,Lys
9
]NT
8-13
, [Lys
8
-(
W
)-Lys
9
]NT
8-13
, [Lys
9
,Trp
11
,Glu
12
]NT
8-13
, and NT
9-13
, adsorbed onto nanometer-sized colloidal
silver particles in an aqueous solution at pH level of the solution 2 are presented. A comparison was made between the struc-
tures of the native and mutated fragments to determine how changes in peptide length and mutations of the structure
in
fl
uenced the NT adsorption properties. Based on the interpretation of the obtained data, we showed that all of the investi-
gated NT fragments, excluding [Lys
9
,Trp
11
,Glu
12
]NT
8-13
, tended to adsorb on the silver surface mainly through the L-tyrosine
residue and the carboxylate group. The Tyr ring lied more-or-less
fl
at on the silver surface. The hydrogen atom from the
phenol group dissociated upon binding. On the other hand, [Lys
9
,Trp
11
,Glu
12
]NT
8-13
bound to this substrate through the close
to vertical co-pyrrole ring of the indole ring (Trp
11
) and
–
COO
-
.
Comparison of the presented data with those obtained earlier for NT allows to suggest that in the case of naturally
occurring neurotensin, both Tyr residues together with the carboxylate group play crucial role in the binding to the nanome-
ter-sized colloidal silver particles. This geometry of binding forces the NT molecule to lay
fl
at on the surface. dc.affiliationpl
Wydział Chemii : Zakład Fizyki Chemicznej dc.contributor.authorpl
Proniewicz, Leonard - 131552 dc.contributor.authorpl
Proniewicz, Edyta - 131481 dc.contributor.authorpl
Pienpinijtham, Prompong dc.contributor.authorpl
Ozaki, Yukihiro dc.contributor.authorpl
Kim, Younkyoo dc.date.accessioned
2015-06-24T07:23:22Z dc.date.available
2015-06-24T07:23:22Z dc.date.issuedpl
2013 dc.description.adminpl
[AB] Proniewicz, Edyta [SAP11017634] 50000141 dc.description.numberpl
1 dc.description.physicalpl
55-62 dc.description.volumepl
44 dc.identifier.doipl
10.1002/jrs.4157 dc.identifier.eissnpl
1097-4555 dc.identifier.issnpl
0377-0486 dc.identifier.uri
http://ruj.uj.edu.pl/xmlui/handle/item/10167 dc.languagepl
eng dc.language.containerpl
eng dc.rights.licence
Bez licencji otwartego dostępu dc.subtypepl
Article dc.titlepl
Influence of backbone length and synthetic mutations on orientation of neurotensin fragments adsorbed onto a colloidal silver surface : SERS studies dc.title.journalpl
Journal of Raman Spectroscopy dc.typepl
JournalArticle dspace.entity.type
Publication Affiliations
Wydział Chemii
Proniewicz, Edyta
Proniewicz, Leonard
No affiliation
Pienpinijtham, Prompong
Ozaki, Yukihiro
Kim, Younkyoo