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The secondary structure of peptides derived from the third intracellular loop of the serpentine-type receptors and its interrelation with their biological activity

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The secondary structure of peptides derived from the third intracellular loop of the serpentine-type receptors and its interrelation with their biological activity

Content Provider	Springer Nature Link
Author	Shpakova, E. A. Skvortsova, E. A. Tarasenko, I. I. Shpakov, A. O.
Copyright Year	2012
Abstract	We and other authors have shown that synthetic peptides corresponding to regions of the third cytoplasmic loop (CL-3) of receptors of the serpentine type are capable of activating G-protein signaling cascades and triggering them in the absence of a hormone. To create selective regulators of hormonal signaling systems on the basis of these peptides, the relationship between their biological activity and secondary structure is studied. It is suggested that the most suitable is the helical conformation, which allows the peptide to effectively interact with signaling proteins. The goal of this study was to test the biological activity and secondary structure of linear peptides that we synthesized and their dimeric and palmitoylated analogs corresponding to the C-terminal region of CL-3 of luteinizing hormone receptor (LHR) and 5-hydroxytryptamine (serotonin) receptor of type 6 (Ser$_{6}$R). It is shown that LHR peptides at micromolar concentrations stimulate the basal activity of adenylyl cyclase (AC) and the GTP-binding of G-proteins in plasma membranes of rat testes, while Ser$_{6}$R peptides activate AC and G-proteins in synaptosomal membranes of rat brain. The action of peptides is tissue-specific and observed in tissues where there are homologous receptors. The most effective were palmitoylated peptides. LHR peptide reduced the AC stimulatory effect of human chorionic gonadotropin, while Ser$_{6}$R peptides, the effect of Ser$_{6}$R-agonist, EMD-386088, and the action of the peptides was not found in the case of nonhomologous receptors. Using circular dichroism spectroscopy, it is shown that in the neutral (pH 7) and acidic (pH 2) medium, all the peptides exist predominantly in the antiparallel β-sheet (37–42%) and disordered conformations (33–35%). In the alkaline medium (pH 10) in the case of palmitoylated peptides the increase of the contribution of the helical conformation to 12–27% was observed. In the presence of trifluoroethanol (10–80%), a helix-forming solvent, the contribution of helical conformation for the majority of peptides was slightly increased (for palmitoylated analogs by 14%); however, in this case, the antiparallel β-sheet and disordered conformation prevailed. The conclusion was drawn that the lack of a clearly expressed ability to form helices in peptides derived from CL-3 of receptors did not significantly affect their activity. This is consistent with the proposed mechanism of peptide action, whereby peptide interacts with the complementary regions of homologous receptor that does not require helix formation.
Starting Page	197
Ending Page	210
Page Count	14
File Format	PDF
ISSN	1990519X
Journal	Cell and Tissue Biology
Volume Number	6
Issue Number	3
e-ISSN	19905203
Language	English
Publisher	SP MAIK Nauka/Interperiodica
Publisher Date	2012-06-14
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	adenylyl cyclase G-protein structure circular dichroism peptide luteinized hormone receptor serotonin serotonin receptor of the sixth type the third cytoplasmic loop Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology

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