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Structural investigation of 3,4-dihydroxyphenylalanine-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 Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 107, no 48, 13396-13402 p.Article in journal (Refereed) Published
Abstract [en]

3,4-Dihydroxyphenylalanine-terminated propanethiol (DOPA-PT), an amino acid DOPA linked to 3-mercaptopropionic acid through an amide bond, is adsorbed and self-assembled to polycrystalline gold surfaces. The structure of the adsorbates was characterized by means of X-ray photoelectron spectroscopy (XPS), infrared reflection−absorption spectroscopy (IRAS), and near-edge X-ray absorption fine structure spectroscopy (NEXAFS). Strong molecular binding of a DOPA derivative on gold surfaces through the sulfur atom was attained. Angle-dependent XPS results showed that the aromatic ring is oriented away from the gold surface. Both IRAS and NEXAFS results showed parallel orientation of the C=O bond of the amide moiety relative to the gold surface. Hydrogen bonding between amide moieties is achieved, and it seemed to provide additional orientation stabilization. Deduced orientation of the amide moiety on the short alkyl chain (or the peptide plane) is assumed to give the average orientation of the main molecular axis. The main molecular axis is estimated to have an average tilt angle of approximately 37° relative to the gold surface normal based on NEXAFS results. The aromatic ring exhibits a preferred orientation with an average tilt angle of about 64°. The experimental results showed that DOPA-thiol with amide linkage is able to self-assemble and form a layered structured film consisting of a layer of alkane chains with a gauche conformation beneath an oriented layer of DOPA.

Place, publisher, year, edition, pages
2003. Vol. 107, no 48, 13396-13402 p.
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:liu:diva-42230DOI: 10.1021/jp030323sLocal ID: 61680OAI: oai:DiVA.org:liu-42230DiVA: diva2:263086
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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Petoral, Rodrigo JrUvdal, Kajsa

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