Interaction of hydrophobic and amphipathic antimicrobial peptides with lipid bicelles

Bortolus, Marco; Dalzini, Annalisa; Toniolo, Claudio; Hahm, Kyung‐Soo; Maniero, Anna Lisa

doi:10.1002/psc.2645

Cited by 23 publications

(42 citation statements)

References 73 publications

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“…Using simulation analysis, we find an orientational order parameter S 20 of 0.439. Similar values were reported by other groups using EPR spectroscopy 52, 54 . The addition of PrP106-126 at low P/L ratios results in noticeable changes of the spectral line shapes (i.e.…”

Section: Resultssupporting

confidence: 92%

“…Similar suppression is observed for the broad peak near 336 mT as a function P/L. Numerical values of the orientational order parameter S 20 for PrP106-126 and two reported peptides, alamethicin and magainin 2 52, 54 , are displayed in Fig. 7B.…”

Section: Resultssupporting

confidence: 71%

“…Compared to isotropic vesicles, orientation-amenable bicelles offer an additional advantage. By magnetically aligning bicelles, the sensitivity of EPR signal to lipid orientation and order is enhanced 52, 54, 115–116 . Effects of administrated peptides on lipid orientational order can be assessed by analysis of spectral line shapes.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, the extent of the reduction of S 20 at different P/L ratios is correlated with the action mode of the peptide. For example, peptides forming barrel-stave pores have a modest impact on the orientational order of lipid acyl chains, whereas peptides forming toroidal pores (or having a detergent-like effect) can cause a strong disordering on lipid chain orientational order 52 . Based on the outlined criteria, the authors proceeded to evaluate the mechanism of membrane disruption caused by AMPs that had not been well-characterized 52 .…”

Section: Discussionmentioning

confidence: 99%

“…Orientations of the principal axes of the diffusion tensor relative to the g tensor reference frame are α D =γ D =0° and β D =33.5°. A non-zero value of the β D angle has been determined previously 52, 54 . It was attributed to the different chain lengths of DMPC (14 carbons long) and the spin label 5-SASL (18 carbons long).…”

Section: Methodsmentioning

confidence: 97%

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Membrane Disruption Mechanism of a Prion Peptide (106–126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy

Pan¹,

Sahoo²,

Dalzini

et al. 2017

J. Phys. Chem. B

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A fragment of the human prion protein spanning residues 106-126 (PrP106-126) recapitulates many essential properties of the disease-causing protein such as amyloidogenicity and cytotoxicity. PrP106-126 has an amphipathic characteristic that resembles many antimicrobial peptides (AMPs). Therefore, the toxic effect of PrP106-126 could arise from a direct association of monomeric peptides with membrane matrix. Several experimental approaches are employed to scrutinize the impacts of monomeric PrP106-126 on model lipid membranes. Porous defects in planar bilayers are observed by using solution atomic force microscopy. Adding cholesterol does not impede defect formation. Force spectroscopy experiment shows that PrP106-126 reduces Young’s modulus of planar lipid bilayers. We use Raman microspectroscopy to study the effect of PrP106-126 on lipid vibrational dynamics. For phosphatidylcholine lipids, PrP106-126 disorders the intra-chain conformation, while the inter-chain interaction is not altered; for phosphatidylethanolamine lipids, PrP106-126 increases the inter-chain interaction, while the intra-chain conformational order remains similar. We explain the observed differences by considering different modes of peptide insertion. Finally, electron paramagnetic resonance spectroscopy shows that PrP106-126 progressively decreases the orientational order of lipid acyl chains in magnetically aligned bicelles. Together, our experimental data support the proposition that monomeric PrP106-126 can disrupt lipid membranes by using similar mechanisms found in AMPs.

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Section: Resultssupporting

confidence: 92%

Section: Resultssupporting

confidence: 71%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 97%

See 3 more Smart Citations

Membrane Disruption Mechanism of a Prion Peptide (106–126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy

Pan¹,

Sahoo²,

Dalzini

et al. 2017

J. Phys. Chem. B

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The fluorescence and infrared absorption probe para‐cyanophenylalanine: Effect of labeling on the behavior of different membrane‐interacting peptides

et al. 2015

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Total syntheses and complete characterizations of singly substituted PheCN -based analogs of alamethicin AlaP, which is active on model and natural membranes, and the TM peptide, which inserts in a transmembrane orientation in lipid bilayers, are reported. The syntheses of the AlaP analogs were performed in solution, while those of TM and its analogs were carried out by solid phase. Using the cyanophenyl fluorescence and infrared (IR) absorption probe, an in-depth investigation of the self-association, membrane-interacting, permeabilizing, and orientation properties of these peptides were conducted. The aromatic residue incorporated induces only a negligible modification to the properties of the parent peptides. The PheCN IR absorption band was located between 2228 and 2230 cm(-1) for all peptides, irrespective of the position of labeling. By contrast, as the width of this band varied significantly with the depth of probe insertion in the bilayer, it could represent a good marker of the PheCN position in phospholipid membranes.

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Insights into peptide‐membrane interactions of newly synthesized, nitroxide‐containing analogs of the peptaibiotic trichogin GAIV using EPR

et al. 2017

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Trichogin GA IV is a short-length (10-amino acid long), mostly hydrophobic, peptaibiotic with an N-terminal fatty acyl chain and a C-terminal 1,2-amino alcohol. A cardinal role of the terminal moieties in the cytotoxic activity of trichogin has been recently found. Previously, peptide orientation and dynamics of trichogin analogs in the membrane were studied using methyl ester derivatives. Therefore, in the present work we synthesized several trichogin analogs with naturally occurring terminal groups to verify whether these moieties have any effect on peptide-membrane interaction. These trichogin analogs, both neutral and carrying a positively charged Lys residue, bear the nitroxide-containing α-amino acid TOAC to study them using EPR spectroscopy. Vesicles were used to investigate orientation and penetration depth of the peptide at room temperature. Bicelles were employed to evaluate the order, dynamics, and orientation of the peptide at a near physiological temperature. In addition, the position of the N-terminal 1-octanoyl chain in the membrane was studied by labeling it with a nitroxide. The secondary structure of the peptides in vesicles was studied by CD spectroscopy showing that they adopt a mostly α-helical structure. In vesicles, the analogs insert below the lipid headgroups with the helix axis oriented parallel to the membrane surface at a peptide-to-lipid (P:L) ratio of 1:100. The presence of the single, positively charged Lys residue does not alter the orientation adopted by the peptides. In bicelles at P:L ratios 1:100 and 1:60, the peptide adopts a transmembrane orientation characterized by a very low orientational order, whereas at a 1:15 P:L ratio it severely disrupts the membrane. Our data shows that overall orientation and insertion in model membranes of the native trichogin GA IV are strictly comparable to those of its methyl ester analogs previously examined.

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Interaction of hydrophobic and amphipathic antimicrobial peptides with lipid bicelles

Cited by 23 publications

References 73 publications

Membrane Disruption Mechanism of a Prion Peptide (106–126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy

Membrane Disruption Mechanism of a Prion Peptide (106–126) Investigated by Atomic Force Microscopy, Raman and Electron Paramagnetic Resonance Spectroscopy

The fluorescence and infrared absorption probe para‐cyanophenylalanine: Effect of labeling on the behavior of different membrane‐interacting peptides

Insights into peptide‐membrane interactions of newly synthesized, nitroxide‐containing analogs of the peptaibiotic trichogin GAIV using EPR

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