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Metal ion interaction with phosphorylated tyrosine analogue monolayers on gold
Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
2006 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 110, no 46, 23410-23416 p.Article in journal (Refereed) Published
Abstract [en]

Phosphorylated tyrosine analogue molecules (pTyr-PT) were assembled onto gold substrates, and the resulting monolayers were used for metal ion interaction studies. The monolayers were characterized by X-ray photoelectron spectroscopy (XPS), infrared reflection−absorption spectroscopy (IRAS), cyclic voltammetry (CV), and electrochemical impedance spectroscopy (EIS), both prior to and after exposure to metal ions. XPS verified the elemental composition of the molecular adsorbate and the presence of metal ions coordinated to the phosphate groups. Both the angle-dependent XPS and IRAS results were consistent with the change in the structural orientation of the pTyr-PT monolayer upon exposure to metal ions. The differential capacitance of the monolayers upon coordination of the metal ions was evaluated using EIS. These metal ions were found to significantly change the capacitance of the pTyr-PT monolayers in contrast to the nonphosphorylated tyrosine analogue (TPT). CV results showed reduced electrochemical blocking capabilities of the phosphorylated analogue monolayer when exposed to metal ions, supporting the change in the structure of the monolayer observed by XPS and IRAS. The largest change in the structure and interfacial capacitance was observed for aluminum ions, compared to calcium, magnesium, and chromium ions. This type of monolayer shows an excellent capability to coordinate metal ions and has a high potential for use as sensing layers in biochip applications to monitor the presence of metal ions.

Place, publisher, year, edition, pages
2006. Vol. 110, no 46, 23410-23416 p.
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:liu:diva-36129DOI: 10.1021/jp064075mLocal ID: 30010OAI: oai:DiVA.org:liu-36129DiVA: diva2:256977
Available from: 2009-10-10 Created: 2009-10-10 Last updated: 2017-12-13
In thesis
1. Bioactive adsorbates on gold surfaces: structural properties and bio-interaction studies
Open this publication in new window or tab >>Bioactive adsorbates on gold surfaces: structural properties and bio-interaction studies
2005 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

This thesis investigates the properties of biomolecular, model adsorbates on gold such as amino acid derivatives, peptides and related organic molecules. Subsequent bin-interaction studies were also conducted. The physico-chemical and structural properties of the adsorbates were characterized using X-ray Photoelectron Spectroscopy (XPS), Infrared-Reflection Absmption Spectroscopy (IRAS) and Near-Edge X-ray Absmption Fine Structures spectroscopy (NEXAFS). Complementary techniques such as Null ellipsometry and Cyclic Voltammetry (CV) were also used. The interaction of the bioactive monolayers with biologically relevant molecules, such as proteins and metal ions, were investigated using Surface Plasmon Resonance (SPR) spectroscopy and Electrochendcallmpedance Spectroscopy (EIS).

The first part of the thesis is directed towards the interaction of bovine-brain G-protein with adsorbates involving arginine residues and receptor-derived peptides mimicking the 2nd and 3rd intracellular (ic) loop of the α2A Adrenergic G-protein coupledreceptor (GPCR). The general aim is to find a peptide sequence that will selectively, with high affinity, interact with the G-protein. The specific aims were to examine the importance of the presence of positively charged arginine residues, to investigate the influence of molecular orientation of the adsorbates, and to verify which intracellular loop has the highest affinity to the G-protein. The investigation involved characterizing the chemical composition and the molecular orientation of Arginine-based dipeptide adsorbates (Arg-Cys and Arg-Cysteandne) and receptor-detived peptides (GPR1R also labeled GPRi3c, GPR1K, GPR1A, GPRi2c, GPRi3n) innnobilized on gold surfaces, followed by G~protein interaction studies. On all the adsorbates subjected to interact with G-proteins, the presence of arginine residues was proven to be of special importance in the affinity of G-proteins. A molecularly"oriented Arg-Cysteamine, with main molecular axis perpendicular to the gold surface, showing more available arginines, attracts more G-proteins as compared to Arg-Cys that has a compact configuration when adsorbed on gold. The peptide adsorbates derived from the third ic loop (GPRi3c and GPRi3n) have higher affinity than peptides derived from the second ic loop (GPRi2c). This shows that this arginine-rich area of the third ic loop has a major influence on the affinity and selectivity of G-proteins.

Place, publisher, year, edition, pages
Linköping: Linköpings universitet, 2005. 76 p.
Series
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 988
National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-30969 (URN)16648 (Local ID)91-8545-775-2 (ISBN)16648 (Archive number)16648 (OAI)
Public defence
2005-12-16, Hörsal Plank, Fysikhuset, Campus Valla, Linköping, 10:15 (Swedish)
Opponent
Available from: 2009-10-09 Created: 2009-10-09 Last updated: 2012-11-23

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Uvdal, KajsaPetoral, Rodrigo JrBjörefors, Fredrik

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