Jagiellonian University Repository

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

pcg.skipToMenu

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

Show full item record

dc.contributor.author Proniewicz, Leonard [SAP11008736] pl
dc.contributor.author Proniewicz, Edyta [SAP11017634] 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.identifier.issn 0377-0486 pl
dc.identifier.uri http://ruj.uj.edu.pl/xmlui/handle/item/10167
dc.language eng 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.type JournalArticle pl
dc.description.physical 55-62 pl
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.description.volume 44 pl
dc.description.number 1 pl
dc.identifier.doi 10.1002/jrs.4157 pl
dc.identifier.eissn 1097-4555 pl
dc.title.journal Journal of Raman Spectroscopy pl
dc.language.container eng pl
dc.affiliation Wydział Chemii : Zakład Fizyki Chemicznej pl
dc.subtype Article pl
dc.rights.original bez licencji pl
.pointsMNiSW [2013 A]: 30


Files in this item

Files Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)