Interfacial properties of the M1 segment of the nicotinic acetylcholine receptor

Ambroggio, Ernesto E.; Villarreal, Marcos Ariel; Montich, Guillermo G.; Rijkers, Dirk T. S.; Planque, Maurits R.R. de; Separovic, Frances; Fidelio, Gerardo D.

doi:10.1016/j.bpc.2005.12.007

Cited by 9 publications

(7 citation statements)

References 33 publications

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“…The surface activity of peptide can also be investigated by experiments on a constant area monitoring the adsorption kinetics of peptide at a clean interface (without lipid) (MagetDana et al 1999;Ambroggio et al 2006;Eeman et al 2006;Dennison et al 2009). The progress of the adsorption depends on ionic strength, pH, temperature and peptide concentration (Seelig 1990;Maget-Dana 1999;Dennison et al 2010).…”

Section: Charge Effect On Lipid Packing Perturbation Induced By Peptimentioning

confidence: 99%

Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides

2017

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The indiscriminate use of conventional antibiotics is leading to an increase in the number of resistant bacterial strains, motivating the search for new compounds to overcome this challenging problem. Antimicrobial peptides, acting only in the lipid phase of membranes without requiring specific membrane receptors as do conventional antibiotics, have shown great potential as possible substituents of these drugs. These peptides are in general rich in basic and hydrophobic residues forming an amphipathic structure when in contact with membranes. The outer leaflet of the prokaryotic cell membrane is rich in anionic lipids, while the surface of the eukaryotic cell is zwitterionic. Due to their positive net charge, many of these peptides are selective to the prokaryotic membrane. Notwithstanding this preference for anionic membranes, some of them can also act on neutral ones, hampering their therapeutic use. In addition to the electrostatic interaction driving peptide adsorption by the membrane, the ability of the peptide to perturb lipid packing is of paramount importance in their capacity to induce cell lysis, which is strongly dependent on electrostatic and hydrophobic interactions. In the present research, we revised the adsorption of antimicrobial peptides by model membranes as well as the perturbation that they induce in lipid packing. In particular, we focused on some peptides that have simultaneously acidic and basic residues. The net charges of these peptides are modulated by pH changes and the lipid composition of model membranes. We discuss the experimental approaches used to explore these aspects of lipid membranes using lipid vesicles and lipid monolayer as model membranes.

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Section: Charge Effect On Lipid Packing Perturbation Induced By Peptimentioning

confidence: 99%

Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides

2017

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“…One can wonder whether the same results can be obtained with these two approaches and which one is most appropriate. There is approximately twice as many papers reporting measurements where peptides are injected into the subphase [105,125,176,192, as compared to papers reporting data after spreading lipid-peptide mixtures at the air-water interface [176-178, 180-185, 190, 191, 193, 194, 218, 220, 229, 289, 295-326]. It is most relevant to find out whether the same peptide structure is obtained when using these two approaches.…”

Section: Spreading the Peptide-lipid Mixture At The Surface Or Injectmentioning

confidence: 99%

“…Monolayers have thus been extensively used to study the orientation and structure of different types of peptides upon lipid binding (see section 4.1 for an extensive review). More specifically, monolayers have additionally been used to characterize the structure and organization of hydrophobic transmembrane peptides such as a transmembrane segment of the nicotinic membrane receptor [176], of signal sequence peptides allowing translocation of proteins to membranes [177], of the gramicidin transmembrane ion channel [178][179][180][181][182][183][184][185][186][187], of a model peptide for an anesthetic-binding membrane protein [188,189], of transmembrane α-helical model peptides [190,191], of transmembrane peptides derived from the domain M of an enzyme [192], of the transmembrane segment of the Vpu protein [193][194][195], as well as of the synaptobrevin 1/VAMP1 and syntaxin 1 [196], and of the N-and C-terminal transmembrane peptides of LRAT [58].…”

Section: Monolayers As a Model Membrane To Study Hydrophobic Transmemmentioning

confidence: 99%

Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins

Lhor¹,

Bernier²,

Horchani³

et al. 2014

Advances in Colloid and Interface Science

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Membrane binding of proteins such as short chain dehydrogenases reductases or tail-anchored proteins relies on their N-and/or C-terminal hydrophobic transmembrane segment. In this review, we propose guidelines to characterize such hydrophobic peptide segments using spectroscopic and biophysical measurements. The secondary structure content of the C-terminal peptides of retinol dehydrogenase 8, RGS9-1 anchor protein, lecithin retinol acyl transferase, and of the N-terminal peptide of retinol dehydrogenase 11 has been deduced by prediction tools from their primary sequence as well as by using infrared or circular dichroism analyses. Depending on the solvent and the solubilization method, significant structural differences were observed, often involving α-helices. The helical structure of these peptides was found to be consistent with their presumed membrane binding. Langmuir monolayers have been used as membrane models to study lipidpeptide interactions. The values of maximum insertion pressure obtained for all peptides using a monolayer of 1,2-dioleoyl-sn-glycero-3-phospho-ethanolamine (DOPE) are larger than the estimated lateral pressure of membranes, thus suggesting that they bind membranes. Polarization modulation infrared reflection absorption spectroscopy has been used to determine the structure and orientation of these peptides in the absence and in the presence of a DOPE monolayer. This lipid induced an increase or a decrease in the organization of the peptide secondary structure. Further measurements are necessary using other lipids to better understand the membrane interactions of these peptides.

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“…In the study presented here, we used solid-state NMR and DPI to analyze the effects of proline substitution in the AMP maculatin 1.1 on the bilayer structure of neutral and net anionic phospholipid membranes. Proline has a specific effect on peptide and protein structure and flexibility (29,(36)(37)(38)(39)(40)(41), and the changes in membrane structure induced by the binding of these peptides reveal the critical role of the proline residue in the disruption of the bilayer structure.…”

Section: Introductionmentioning

confidence: 99%

Proline Facilitates Membrane Insertion of the Antimicrobial Peptide Maculatin 1.1 via Surface Indentation and Subsequent Lipid Disordering

Fernandez

Lee

Sani

et al. 2013

Biophysical Journal

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The role of proline in the disruption of membrane bilayer structure upon antimicrobial peptide (AMP) binding was studied. Specifically, (31)P and (2)H solid-state NMR and dual polarization interferometry (DPI) were used to analyze the membrane interactions of three AMPs: maculatin 1.1 and two analogs in which Pro-15 is replaced by Gly and Ala. For NMR, deuterated dimyristoylphosphatidylcholine (d54-DMPC) and d54-DMPC/dimyristoylphosphatidylglycerol (DMPG) were used to mimic eukaryotic and prokaryotic membranes, respectively. In fluid-phase DMPC bilayer systems, the peptides interacted primarily with the bilayer surface, with the native peptide having the strongest interaction. In the mixed DMPC/DMPG bilayers, maculatin 1.1 induced DMPG phase separation, whereas the analogs promoted the formation of isotropic and lipid-enriched phases with an enhanced effect relative to the neutral DMPC bilayers. In gel-phase DMPC vesicles, the native peptide disrupted the bilayer via a surface mechanism, and the effect of the analogs was similar to that observed in the fluid phase. Real-time changes in bilayer order were examined via DPI, with changes in bilayer birefringence analyzed as a function of the peptide mass bound to the bilayer. Although all three peptides decreased the bilayer order as a function of bound concentration, maculatin 1.1 caused the largest change in bilayer structure. The NMR data indicate that maculatin 1.1 binds predominantly at the surface regions of the bilayer, and both NMR and DPI results indicate that this binding leads to a drop in bilayer order. Overall, the results demonstrate that the proline at residue 15 plays a central role in the membrane interaction of maculatin 1.1 by inducing a significant change in membrane order and affecting the ability of the bilayer to recover from structural changes induced by the binding and insertion of the peptide.

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Interfacial properties of the M1 segment of the nicotinic acetylcholine receptor

Cited by 9 publications

References 33 publications

Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides

Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides

Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins

Proline Facilitates Membrane Insertion of the Antimicrobial Peptide Maculatin 1.1 via Surface Indentation and Subsequent Lipid Disordering

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