Liposome destabilization induced by synthetic lipopeptides corresponding to envelope and non-structural domains of GBV-C/HGV virus. Conformational requirements for leakage

Fernández-Vidal, Mónica; Rojo, N.; Herrera, Elena; Gómara, María J.; Haro, Isabel

doi:10.1016/j.bpc.2007.10.009

Cited by 4 publications

(3 citation statements)

References 49 publications

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“…So the ␣-helical content is lower in this case. On the other hand this is a normal behavior observed in other E1 peptides that were studied (Fernández-Vidal et al, 2008). First, results show that P18 has a high percentage of ␣-helix compared to the rest and the percentage obtained for P10 is equal to that obtained for HIV-1 FP; these results are coherent with those obtained in Table 1, showing that P10 and P18 behave different from P7 and P8, and that P10 has some similarities with HIV-1 FP.…”

Section: Circular Dichroismsupporting

confidence: 81%

Physicochemical characterization of GBV-C E1 peptides as potential inhibitors of HIV-1 fusion peptide: Interaction with model membranes

Sánchez-Martín¹,

Cruz²,

Busquets³

et al. 2012

International Journal of Pharmaceutics

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Four peptide sequences corresponding to the E1 protein of GBV-C: NCCAPEDIGFCLEGGCLV (P7), APEDIGFCLEGGCLVALG (P8), FCLEGGCLVALGCTICTD (P10) and QAGLAVRPGKSAAQLVGE (P18) were studied as they were capable of interfering with the HIV-1 fusion peptide (HIV-1 FP). In this work, the surface properties of the E1 peptide sequences are investigated and their physicochemical characterization is done by studying their interaction with model membranes; moreover, their mixtures with HIV-1 FP were also studied in order to observe whether they are capable to modify the HIV-1 FP interaction with model membranes as liposomes or monolayers. Physicochemical properties of peptides (pI and net charge) were predicted showing similarities between P7 and P8, and P10 and HIV-1 FP, whereas P18 appears to be very different from the rest. Circular dichroism experiments were carried out showing an increase of the percentage of α-helix of P7 and P8 when mixed with HIV-1 FP corroborating a conformational change that could be the cause of their inhibition ability. Penetration experiments show that all the peptides can spontaneously insert into phospholipid membranes. Analysis of compression isotherms indicates that the peptides interact with phospholipids and the E1 peptides modify the compression isotherms of HIV-1 FP, but there is one of the peptides that excelled as the best candidate for inhibiting the activity of HIV-1 FP, P7, and therefore, that could be potentially used in future anti-HIV-1 research.

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Section: Circular Dichroismsupporting

confidence: 81%

Physicochemical characterization of GBV-C E1 peptides as potential inhibitors of HIV-1 fusion peptide: Interaction with model membranes

Sánchez-Martín¹,

Cruz²,

Busquets³

et al. 2012

International Journal of Pharmaceutics

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“…Fluorescence leakage experiments were performed as previously described (31,32). For the 8-aminonaphthalene-1,3,6-trisulfonic acid (ANTS)-N,N 0p-xylene-bis-pyridinium bromide (DPX) leakage assay, $15 mg of DPPC was dissolved in a mixture of chloroform and methanol (3:1), which was subsequently removed under a stream of N 2 , whereas the remainder was vacuum dried for 8 h. Buffer (1 mL) containing 12.5 mM ANTS (Molecular Probes, Eugene, OR), 20 mM NaCl, and 5 mM HEPES was added to the dry lipid, and the suspension was frozen and thawed 10 times to assure maximal entrapment before extrusion.…”

Section: Fluorescence Leakage Experimentsmentioning

confidence: 99%

Endocytosis Is a Key Mode of Interaction between Extracellular β-Amyloid and the Cell Membrane

Shi

Zhu

Lan

et al. 2020

Biophysical Journal

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Interactions between amyloid-b peptide (Ab) and the cell membrane include interaction with membrane lipids and binding to membrane receptors, both of which are considered to be the toxicity mechanisms of Ab. However, it is unclear whether both mechanisms lead to cytotoxicity. Thus, we aimed to analyze these two mechanisms of Ab42 interaction with cell membranes under different Ab aggregation states. To this end, model membrane experiments were conducted. Quantitative analysis of Ab42 monomers or oligomers bound to the membrane of neuro-2a cells was also performed, and laser confocal microscopy was employed to assess endocytosis of FITC-Ab42 monomers or oligomers by neuro-2a cells. We found that the binding capacity of Ab42 to membrane lipids was weak and that the amount of Ab42 bound to membrane lipids was low. Moreover, clathrin-mediated endocytosis of Ab42 oligomers by neuro-2a cells was observed. Endocytosis serves as a key mode of interaction between extracellular Ab42 and neurons. These findings provide insights into the mechanisms underlying Ab oligomer metabolism.

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“…Dequenching of co-encapsulated ANTS and DPX fluorescence in LUVs (obtained as described in Section 2.2) was measured to assess the release of vesicular contents to the medium, as described in the literature [44]. Briefly, a lipid suspension was diluted in 5 mM Hepes (pH 7.4) containing 100 mM NaCl to give a final lipid concentration of 0.1 mM.…”

Section: Methodsmentioning

confidence: 99%

Contribution of the Tyr-1 in Plantaricin149a to Disrupt Phospholipid Model Membranes

Lopes

Gómara

Haro

et al. 2013

IJMS

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Plantaricin149a (Pln149a) is a cationic antimicrobial peptide, which was suggested to cause membrane destabilization via the carpet mechanism. The mode of action proposed to this antimicrobial peptide describes the induction of an amphipathic α-helix from Ala7 to Lys20, while the N-terminus residues remain in a coil conformation after binding. To better investigate this assumption, the purpose of this study was to determine the contributions of the Tyr1 in Pln149a in the binding to model membranes to promote its destabilization. The Tyr to Ser substitution increased the dissociation constant (KD) of the antimicrobial peptide from the liposomes (approximately three-fold higher), and decreased the enthalpy of binding to anionic vesicles from −17.2 kcal/mol to −10.2 kcal/mol. The peptide adsorption/incorporation into the negatively charged lipid vesicles was less effective with the Tyr1 substitution and peptide Pln149a perturbed the liposome integrity more than the analog, Pln149S. Taken together, the peptide-lipid interactions that govern the Pln149a antimicrobial activity are found not only in the amphipathic helix, but also in the N-terminus residues, which take part in enthalpic contributions due to the allocation at a lipid-aqueous interface.

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Liposome destabilization induced by synthetic lipopeptides corresponding to envelope and non-structural domains of GBV-C/HGV virus. Conformational requirements for leakage

Cited by 4 publications

References 49 publications

Physicochemical characterization of GBV-C E1 peptides as potential inhibitors of HIV-1 fusion peptide: Interaction with model membranes

Physicochemical characterization of GBV-C E1 peptides as potential inhibitors of HIV-1 fusion peptide: Interaction with model membranes

Endocytosis Is a Key Mode of Interaction between Extracellular β-Amyloid and the Cell Membrane

Contribution of the Tyr-1 in Plantaricin149a to Disrupt Phospholipid Model Membranes

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