Related ArticlesHelix Fraying and Lipid-Dependent Structure of a Short Amphipathic Membrane-Bound Peptide Revealed by Solid-State NMR.
J Phys Chem B. 2018 06 14;122(23):6236-6250
Authors: Strandberg E, Grau-Campistany A, Wadhwani P, Bürck J, Rabanal F, Ulrich AS
Abstract
The amphipathic ?-helical peptide KIA14 [(KIAGKIA)2-NH2] was studied in membranes using circular dichroism and solid-state NMR spectroscopy to obtain global as well as local structural information. By analyzing 2H NMR data from 10 analogues of KIA14 that were selectively labeled with Ala- d3, those positions that are properly folded into a helix could be determined within the membrane-bound peptide. The N-terminus was found to be unraveled, whereas positions 4-14 formed an ideal helix all the way to the C-terminus. The helicity did not change when Gly residues were replaced by Ala- d3 but was reduced when Ile was replaced, indicating that large hydrophobic residues are required for membrane binding and helix formation. The reduced helicity was strongly correlated with a decrease in peptide-induced leakage from lipid vesicles. The orientation of the short KIA14 peptide was assessed in several lipid systems and compared with that of the longer KIA21 sequence [(KIAGKIA)3-NH2]. In 1,2-dioleoyl- sn-glycero-3-phosphatidylcholine, both peptides are aligned flat on the membrane surface, whereas in 1,2-dimyristoyl- sn-glycero-3-phosphatidylcholine (DMPC)/1-myristoyl-2-hydroxy- sn-glycero-3-phosphatidylcholine (lyso-MPC) both are inserted into the membrane in an upright orientation. These two types of lipid systems had been selected for their strongly negative and positive spontaneous curvature, respectively. We propose that in these cases, the peptide orientation is largely determined by the lipid properties. On the other hand, in plain DMPC and 1,2-dilauroyl- sn-glycero-3-phosphatidylcholine, which have only a slight positive curvature, a marked difference in orientation is evident: the short KIA14 lies almost flat on the membrane surface, whereas the longer KIA21 is more tilted. We thus propose that out of the lipid systems tested here, DMPC (with hardly any curvature) is the least biased lipid system in which peptide orientation and realignment can be studied, allowing to compare and discriminate the intrinsic effects of the properties of the peptides as such.
[NMR paper] Dynamic Structure and Orientation of Melittin Bound to Acidic Lipid Bilayers, As Revealed by Solid-State NMR and Molecular Dynamics Simulation.
Dynamic Structure and Orientation of Melittin Bound to Acidic Lipid Bilayers, As Revealed by Solid-State NMR and Molecular Dynamics Simulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Dynamic Structure and Orientation of Melittin Bound to Acidic Lipid Bilayers, As Revealed by Solid-State NMR and Molecular Dynamics Simulation.
J Phys Chem B. 2017 03 02;121(8):1802-1811
Authors: Norisada K, Javkhlantugs N, Mishima D, Kawamura I, Saitô H, Ueda K, Naito A
...
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[NMR paper] Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
Related Articles Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state.
J Mol Biol. 2013 Nov 15;
Authors: Sackett K, Nethercott MJ, Zheng Z, Weliky DP
Abstract
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although...
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Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel ? sheet fusion peptide structure in the final six-helix bundle state
Publication date: Available online 16 November 2013
Source:Journal of Molecular Biology</br>
Author(s): Kelly Sackett , Matthew J. Nethercott , Zhaoxiong Zheng , David P. Weliky</br>
The HIV gp41 protein catalyzes fusion between viral and target cell membranes. Although the ~20-residue N-terminal fusion peptide (FP) region is critical for fusion, the structure of this region is not...
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[NMR paper] Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy.
Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy.
Related Articles Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy.
Biochim Biophys Acta. 2013 Oct 18;
Authors: Zhang L, Liu L, Maltsev S, Lorigan GA, Dabney-Smith C
Abstract
The chloroplast twin arginine translocation (cpTat) system transports highly folded precursor proteins into the thylakoid lumen using...
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[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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Dynamic Nuclear Polarization-Enhanced Solid-State NMR of a 13C-Labeled Signal Peptide Bound to Lipid-Reconstituted Sec Translocon
Dynamic Nuclear Polarization-Enhanced Solid-State NMR of a 13C-Labeled Signal Peptide Bound to Lipid-Reconstituted Sec Translocon
Lenica Reggie, Jakob J. Lopez, Ian Collinson, Clemens Glaubitz and Mark Lorch
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja209378h/aop/images/medium/ja-2011-09378h_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja209378h
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
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Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Biophys J. 2010 Nov 17;99(10):3282-9
Authors: Toraya S, Javkhlantugs N, Mishima D, Nishimura K, Ueda K, Naito A
Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to...