Influence of backbone length and synthetic mutations on orientation of neurotensin fragments adsorbed onto a colloidal silver surface : SERS studies

2013
journal article
article
4
dc.abstract.enNeurotensin (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.affiliationWydział Chemii : Zakład Fizyki Chemicznejpl
dc.contributor.authorProniewicz, Leonard - 131552 pl
dc.contributor.authorProniewicz, Edyta - 131481 pl
dc.contributor.authorPienpinijtham, Prompongpl
dc.contributor.authorOzaki, Yukihiropl
dc.contributor.authorKim, Younkyoopl
dc.date.accessioned2015-06-24T07:23:22Z
dc.date.available2015-06-24T07:23:22Z
dc.date.issued2013pl
dc.description.admin[AB] Proniewicz, Edyta [SAP11017634] 50000141pl
dc.description.number1pl
dc.description.physical55-62pl
dc.description.volume44pl
dc.identifier.doi10.1002/jrs.4157pl
dc.identifier.eissn1097-4555pl
dc.identifier.issn0377-0486pl
dc.identifier.urihttp://ruj.uj.edu.pl/xmlui/handle/item/10167
dc.languageengpl
dc.language.containerengpl
dc.rights.licencebez licencji
dc.subtypeArticlepl
dc.titleInfluence of backbone length and synthetic mutations on orientation of neurotensin fragments adsorbed onto a colloidal silver surface : SERS studiespl
dc.title.journalJournal of Raman Spectroscopypl
dc.typeJournalArticlepl
dspace.entity.typePublication
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
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

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