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231223s2007 xx ||||| 00| ||eng c |
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|a pubmed24n0571.xml
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|a (DE-627)NLM171392167
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|a (NLM)17622157
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Balau, Luminita Savitchi
|e verfasserin
|4 aut
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| 245 |
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|a Mixed monolayers to promote g-protein adsorption
|b alpha2A-adrenergic receptor-derived peptides coadsorbed with formyl-terminated oligopeptides
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|c 2007
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 02.10.2007
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|a Date Revised 18.11.2010
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Pure and mixed monolayers of a synthetic peptide, GPR-i3n, derived from the third intracellular loop of the alpha2 adrenergic receptor and a shorter inactive oligopeptide, N-formyl-(Gly)3-(Cys) (called 3GC), were prepared on gold surfaces. The mixing ratio of the GPR-i3n and 3GC was used to control G-protein binding capability. The GPR-i3n peptide is specially designed for bovine G-protein selectivity and has been proven to have high affinity to G-proteins [Vahlberg, C.; Petoral, R. M., Jr.; Lindell, C.; Broo, K.; Uvdal, K. Langmuir 2006, 22 (17), 7260-7264]. Pure 3GC monolayers show very low protein adsorption capability. In this study, 3GC is chosen as a coadsorbent, with the aim to induce molecular conformational changes during monolayer formation to enhance G-protein adsorption. A full characterization of the mixed monolayers was done. The monolayer thickness and the mass-related surface coverage for both GPR-i3n and 3GC were investigated using radio labeling. The GPR-i3n was labeled by 125I-targeting tyrosine, and the activity was measured by using radioimmunoassay (RIA). The formation and chemical composition of GPR-i3n and 3GC monolayers were investigated using X-ray photoelectron spectroscopy, and it is shown that both GPR-i3n and 3GC bind chemically to the gold surface. The interaction between the mixed monolayers and G-proteins was investigated by means of real-time surface plasmon resonance. There is a higher protein binding capacity to the monolayer when the GPR-i3n peptide is intermixed with the 3GC coadsorbent, despite the fact that the 3GC itself has a very low G-protein binding capability. This supports a molecular reorientation at the surface, while 3GC is intermixed with GPR-i3n
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a ADRA2A protein, human
|2 NLM
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| 650 |
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|a Membranes, Artificial
|2 NLM
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| 650 |
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|a Oligopeptides
|2 NLM
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| 650 |
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|a Receptors, Adrenergic, alpha-2
|2 NLM
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|a Gold
|2 NLM
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| 650 |
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|a 7440-57-5
|2 NLM
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| 650 |
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|a GTP-Binding Proteins
|2 NLM
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| 650 |
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|a EC 3.6.1.-
|2 NLM
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| 700 |
1 |
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|a Vahlberg, Cecilia
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Petoral, Rodrigo M
|c Jr
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Uvdal, Kajsa
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 23(2007), 16 vom: 31. Juli, Seite 8474-9
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
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|g volume:23
|g year:2007
|g number:16
|g day:31
|g month:07
|g pages:8474-9
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_NLM
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|a GBV_ILN_22
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|a GBV_ILN_350
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|a GBV_ILN_721
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|a AR
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|d 23
|j 2007
|e 16
|b 31
|c 07
|h 8474-9
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