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XPS and NEXAFS study of tyrosine-terminated propanethiol assembled on gold
Linköping University, Department of Physics, Chemistry and Biology, Applied Physics. Linköping University, The Institute of Technology.
Linköping University, Department of Physics, Chemistry and Biology, Applied Physics. Linköping University, The Institute of Technology.
2003 (English)In: Journal of Electron Spectroscopy and Related Phenomena, ISSN 0368-2048, E-ISSN 1873-2526, Vol. 128, no 2-3, 159-164 p.Article in journal (Refereed) Published
Abstract [en]

Tyrosine-terminated propanethiol (TPT), tyrosine linked to 3-mercaptopropionic acid through an amide bond, is adsorbed to gold surfaces. The adsorbates are characterized by means of X-ray photoelectron spectroscopy (XPS) and near-edge X-ray absorption fine structure spectroscopy (NEXAFS). XPS is used to investigate the chemical binding and electronic structure of the monolayer. Strong molecular binding of the tyrosine derivative on the gold surface through the sulfur atom is attained. Angle-dependent XPS results shows that TPT molecules are oriented with the sulfur atoms molecularly oriented close to the gold surface and that the phenol moiety is oriented away from the gold surface. Average orientation of the adsorbate on gold is deduced using the NEXAFS results. It shows that the main molecular axis is tilted approximately 38° relative to the Au surface normal. The ring plane of the phenol moiety exhibits a preferential orientation with an average tilt angle of the normal of the ring plane from the surface normal of about 60°.

Place, publisher, year, edition, pages
2003. Vol. 128, no 2-3, 159-164 p.
Keyword [en]
NEXAFS, Tyrosine, XPS
National Category
Engineering and Technology
Identifiers
URN: urn:nbn:se:liu:diva-46570DOI: 10.1016/S0368-2048(02)00271-2OAI: oai:DiVA.org:liu-46570DiVA: diva2:267466
Available from: 2009-10-11 Created: 2009-10-11 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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Petoral, Rodrigo JrUvdal, Kajsa

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