[NMR paper] Arginine-, D-arginine-vasopressin, and their inverso analogues in micellar and liposomic models of cell membrane: CD, NMR, and molecular dynamics studies.
Arginine-, D-arginine-vasopressin, and their inverso analogues in micellar and liposomic models of cell membrane: CD, NMR, and molecular dynamics studies.
Related ArticlesArginine-, D-arginine-vasopressin, and their inverso analogues in micellar and liposomic models of cell membrane: CD, NMR, and molecular dynamics studies.
Eur Biophys J. 2015 Dec;44(8):727-43
Authors: Lubecka EA, Sikorska E, Sobolewski D, Prahl A, Slaninová J, Ciarkowski J
Abstract
We describe the synthesis, pharmacological properties, and structures of antidiuretic agonists, arginine vasopressin (AVP) and [D-Arg(8)]-vasopressin (DAVP), and their inverso analogues. The structures of the peptides are studied based on micellar and liposomic models of cell membranes using CD spectroscopy. Additionally, three-dimensional structures in mixed anionic-zwitterionic micelles are obtained using NMR spectroscopy and molecular dynamics simulations. NMR data have shown that AVP and DAVP tend to adopt typical of vasopressin-like peptides ?-turns: in the 2-5 and 3-6 fragments. The inverso-analogues also adopt ?-turns in the 3-6 fragments. For this reason, their inactivity seems to be due to the difference in side chains orientations of Tyr(2), Phe(3), and Arg(8), important for interactions with the receptors. Again, the potent antidiuretic activity of DAVP can be explained by CD data suggesting differences in mutual arrangement of the aromatic side chains of Tyr(2) and Phe(3) in this peptide in liposomes rather than of native AVP. In the presence of liposomes, the smallest conformational changes of the peptides are noticed with DPPC and the largest with DPPG liposomes. This suggests that electrostatic interactions are crucial for the peptide-membrane interactions. We obtained similar, probably active, conformations of the antidiuretic agonists in the mixed DPC/SDS micelles (5:1) and in the mixed DPPC/DPPG (7:3) liposomes. Thus it can be speculated that the anionic-zwitterionic liposomes as well as the anionic-zwitterionic micelles, mimicking the eukaryotic cell membrane environment, partially restrict conformational freedom of the peptides and probably induce conformations resembling those of biologically relevant ones.
[NMR paper] Structure and dynamics of the two amphipathic arginine-rich peptides RW9 and RL9 in a lipid environment investigated by solid-state NMR and MD simulations.
Structure and dynamics of the two amphipathic arginine-rich peptides RW9 and RL9 in a lipid environment investigated by solid-state NMR and MD simulations.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure and dynamics of the two amphipathic arginine-rich peptides RW9 and RL9 in a lipid environment investigated by solid-state NMR and MD simulations.
Biochim Biophys Acta. 2013 Feb;1828(2):824-33
Authors: Witte K, Olausson BE, Walrant A, Alves ID, Vogel A
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Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translo
Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy.
Related Articles Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy.
J Am Chem Soc. 2010 Oct 26;
Authors: Walther TH, Grage SL, Roth N, Ulrich AS
The twin-arginine translocase (Tat) provides protein export in bacteria and plant chloroplasts and is capable of transporting fully folded...
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Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Transloca
Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy
Torsten H. Walther, Stephan L. Grage, Nadine Roth and Anne S. Ulrich
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja106963s/aop/images/medium/ja-2010-06963s_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja106963s
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http://feeds.feedburner.com/~r/acs/jacsat/~4/w34WC8p2mzY
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[NMR paper] 1H/15N HSQC NMR studies of ligand carboxylate group interactions with arginine residu
1H/15N HSQC NMR studies of ligand carboxylate group interactions with arginine residues in complexes of brodimoprim analogues and Lactobacillus casei dihydrofolate reductase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles 1H/15N HSQC NMR studies of ligand carboxylate group interactions with arginine residues in complexes of brodimoprim analogues and Lactobacillus casei dihydrofolate reductase.
Biochemistry. 1999 Feb 16;38(7):2127-34
Authors: Morgan WD, Birdsall B, Nieto PM, Gargaro AR, Feeney J
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Arginine-, D-arginine-vasopressin, and their inverso analogues in micellar and liposomic models of cell membrane: CD, NMR, and molecular dynamics studies.
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