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Synthesis and Spectroscopic Characterization of Photo-affinity Peptide Ligands to Study RhodopsinG Protein Interaction
- Source :
- Photochemistry and Photobiology. 84:831-838
- Publication Year :
- 2008
- Publisher :
- Wiley, 2008.
-
Abstract
- G protein-coupled receptors (GPCRs) are involved in the control of virtually all aspects of our behavior and physiology. Activated receptors catalyze nucleotide exchange in heterotrimeric G proteins (composed of alpha.GDP, beta and gamma subunits) on the inner surface of the cell membrane. The GPCR rhodopsin and the G protein transducin (G(t)) are key proteins in the early steps of the visual cascade. The main receptor interaction sites on G(t) are the C-terminal tail of the G(t)alpha-subunit and the farnesylated C-terminal tail of the G(t)gamma-subunit. Synthetic peptides derived from these C-termini specifically bind and stabilize the active rhodopsin conformation (R*). Here we report the synthesis of R*-interacting peptides containing photo-reactive groups with a specific isotope pattern, which can facilitate detection of cross-linked products by mass spectrometry. In a preliminary set of experiments, we characterized such peptides derived from the farnesylated G(t)gamma C-terminus (G(t)gamma(60-71)far) in terms of their capability to bind R*. Here, we describe novel peptides with photo-affinity labels that bind R* with affinities similar to that of the native G(t)gamma(60-71)far peptide. Such peptides will enable an improved experimental strategy to probe rhodopsin-G(t) interaction and to map so far unknown interaction sites between both proteins.
- Subjects :
- Models, Molecular
Rhodopsin
Photochemistry
Protein Conformation
G protein
Peptide
Biology
Biochemistry
Drug Stability
GTP-Binding Proteins
Heterotrimeric G protein
Amino Acid Sequence
Physical and Theoretical Chemistry
G protein-coupled receptor
chemistry.chemical_classification
G protein-coupled receptor kinase
General Medicine
Kinetics
Protein Subunits
G beta-gamma complex
chemistry
biology.protein
Transducin
Peptides
Subjects
Details
- ISSN :
- 17511097 and 00318655
- Volume :
- 84
- Database :
- OpenAIRE
- Journal :
- Photochemistry and Photobiology
- Accession number :
- edsair.doi.dedup.....084b7d1d6532d0713c23919f3ac6b57f