G-protein interactions with receptor-derived peptides chemisorbed on gold
2003 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 19, no 24, 10304-10309 p.Article in journal (Refereed) Published
Interactions between the functional bovine brain G-protein and receptor-derived peptidea chemically adsorbed on gold surfaces are studied. The peptides are designed to mimic the third ic-loop (aa 361-373) of the Alpha 2a-adrenergic receptor (α 2AR). These segments are linked to a surface using the thiol-gold chemistry, and the protein interaction studies are conducted to investigate the key function of recognition. The chemical composition and binding strength of the peptide monolayers onto a gold surface are characterized using X-ray photoelectron spectroscopy and infrared (IR) spectroscopy. Strong molecular binding of the adsorbates to the gold surface is attained, and the presence of amide-related IR vibrations verified the composition of the peptides. Bovine brain G-protein adsorption studies on these molecular monolayers are performed using the surface plasmon resonance technique. The arginine-rich peptide, which is a direct mimicry of the receptor, has a higher affinity for G-protein than the lysine-rich and alanine-rich derived peptides, showing that arginine residue has special importance for the G-protein interaction with the receptor.
Place, publisher, year, edition, pages
2003. Vol. 19, no 24, 10304-10309 p.
Engineering and Technology
IdentifiersURN: urn:nbn:se:liu:diva-46427DOI: 10.1021/la035046vOAI: oai:DiVA.org:liu-46427DiVA: diva2:267323