Interaction of short modified peptides deriving from glycoprotein gp36 of feline immunodeficiency virus with phospholipid membranes

D’Errico, Gerardino; Vitiello, Giuseppe; D’Ursi, Anna Maria; Marsh, Derek

doi:10.1007/s00249-009-0454-9

Cited by 16 publications

(18 citation statements)

References 43 publications

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“…Each molecule of gH626-644 interacts with a maximum of 15 lipids. On a per-residue basis, this value corresponds to~0.8 lipids per amino acid, a stoichiometry similar to that obtained for two peptides derived from the fusion glycoprotein gp41 of FIV [52,53], whose mechanism of interaction with lipid bilayers has been established to be surface adsorption. In the case of gB632-650, peptide-lipid titration by EPR indicates that a single peptide molecule interacts with a smaller number of lipids (~5), as is expected in the case of peptide penetration in a transverse membrane orientation.…”

Section: Discussionsupporting

confidence: 69%

Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes

Vitiello

Falanga

Galdiero

et al. 2011

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Lipid membranes play a key role in the viral life cycle. Enveloped viruses particularly require a sequence of fusion and fission events between the viral envelope and the target membranes for entry into the cell and egress from it. These processes are controlled by one or more viral glycoproteins that undergo conformational changes favoring the necessary micro- and mesoscopic lipid re-arrangements. Multiple regions from these glycoproteins are thought to interact with the membranes, according to a concerted mechanism, in order to generate the distortion necessary for fusion. In this work, we perform an EPR study on the role played by the membrane composition in tuning the interaction between lipid bilayers and two peptides, gH626-644 and gB632-650, that are highly fusogenic fragments of the gH and gB glycoproteins of herpes simplex virus. Our results show that both peptides interact with lipid bilayers, perturbing the local lipid packing. gH626-644 localizes close to the hydrophilic bilayer surface, while gB632-650 penetrates deeply into the membrane. Chain perturbation by the peptides increases in the presence of charged phospholipids. Finally, cholesterol does not alter the ability of gB632-650 to penetrate deeply in the membrane, whereas it limits penetration of the gH626-644 peptide to the more external layer. The different modes of interaction result in a higher fusogenic ability of gB632-650 towards cholesterol-enriched membranes, as demonstrated by lipid mixing assays. These results suggest that the mechanism of action of the gH and gB glycoproteins is modulated by the properties and composition of the phospholipid bilayer.

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Section: Discussionsupporting

confidence: 69%

Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes

Vitiello

Falanga

Galdiero

et al. 2011

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…Truncations or scrambling of C8, or mutation of the Trp residues to Ala, cause a severe reduction or abrogation of activity. In addition, C8 has an ability to bind to membranes, and substitutions of Trp to less hydrophobic amino acids reduce membrane-binding as well as antiviral activity [176]. Co-incubation of virus and C8 with a peptide corresponding to part of the FP and FP-PR of gp36 was found to completely block the antiviral activity of C8 [174].…”

Section: Mper Peptidesmentioning

confidence: 98%

Targeting HIV-1 gp41 in Close Proximity to the Membrane Using Antibody and Other Molecules

Gach¹,

Leaman²,

Zwick³

2011

CTMC

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HIV-1 envelope glycoprotein (Env) spikes are supported at the viral membrane interface by a highly conserved and hydrophobic region of gp41, designated the membrane-proximal external region (MPER). The MPER is mandatory for infection of host cells by HIV-1, and is the target of some of the most broadly neutralizing antibodies described to date. As such, the MPER is also of considerable interest for HIV vaccine design. However, structural models indicate that the MPER assumes distinct conformations prior to and leading up to Env-mediated fusion. Thus, the more of these distinct conformations that antibodies and inhibitors can recognize will likely be the better for antiviral potency. In addition to its flexibility, the MPER is lipophilic and its accessibility to bulky macromolecules is limited by steric and kinetic blocks that present particular challenges for eliciting HIV-1 neutralizing antibodies. Moreover, the ability of the MPER and viral membrane to combine as a complex has critical mechanistic implications for molecules that target lipid-bound and/or unbound states. Interestingly, membrane affinity frequently appears to enhance the potency of both fusion inhibitors and antibodies to different sites on gp41. We therefore highlight mechanisms to be harnessed in targeting membraneproximal sites on HIV gp41 for both vaccine and fusion inhibitor design. Such design efforts will likely need to draw upon knowledge of MPER structure and function, and may in turn inform analogous approaches to MPERs of other enveloped viruses and systems.

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“…To quantitatively analyze the spectra, the values of the outer hyperfine splitting, 2A max , were determined by measuring the difference between the low-field maximum and the high-field minimum, using a home-made MATLAB-based software routine. In general, 2A max is dependent on both the amplitude (i.e., order) and the rate of chain rotational motion and is therefore a useful parameter for characterizing chain dynamics, as determined by local ordering, in phospholipid membranes60. It is a sensitive means for detecting and quantifying lipid bilayer interactions with guest molecules, as previously demonstrated61.…”

Section: Resultsmentioning

confidence: 88%

Investigating the Neuroprotective Effects of Turmeric Extract: Structural Interactions of β-Amyloid Peptide with Single Curcuminoids

Randino

Grimaldi

Persico

et al. 2016

Sci Rep

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A broad biophysical analysis was performed to investigate the molecular basis of the neuroprotective action of Curcuma longa extracts in Alzheimer’s disease. By combining circular dichroism and electron paramagnetic resonance experiments with molecular modeling calculations, the minor components of Curcuma longa extracts, such as demethoxycurcumin (2, DMC), bisdemethoxycurcumin (3, BDMC) and cyclocurcumin (4, CYC), were analyzed in a membrane environment mimicking the phospholipid bilayer. Our study provides the first evidence on the relative role of single curcuminoids interacting with Aβ-peptide. When the CYC and curcumin metabolite tetrahydrocurcumin (5, THC) were inserted into an anionic lipid solution, a significant modification of the Aβ CD curves was detected. These data were implemented by EPR experiments, demonstrating that CYC reaches the inner part of the bilayer, while the other curcuminoids are localized close to the membrane interface. Computational studies provided a model for the curcuminoid-Aβ interaction, highlighting the importance of a constrained “semi-folded” conformation to interact with Aβ analogously to the pattern observed in α-helical coiled-coil peptide structures. This combined approach led to a better understanding of the intriguing in vitro and in vivo activity of curcuminoids as anti-Alzheimer agents, paving a new path for the rational design of optimized druggable analogues.

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Interaction of short modified peptides deriving from glycoprotein gp36 of feline immunodeficiency virus with phospholipid membranes

Cited by 16 publications

References 43 publications

Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes

Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes

Targeting HIV-1 gp41 in Close Proximity to the Membrane Using Antibody and Other Molecules

Investigating the Neuroprotective Effects of Turmeric Extract: Structural Interactions of β-Amyloid Peptide with Single Curcuminoids

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