Aurelia Apetrei

Learn More
Mustard oil (MO) is a plant-derived irritant that has been extensively used in experimental models to induce pain and inflammation. The noxious effects of MO are currently ascribed to specific activation of the cation channel TRPA1 in nociceptive neurons. In contrast to this view, we show here that the capsaicin receptor TRPV1 has a surprisingly large(More)
BACKGROUND Antimicrobial agents, with different pore-formation mechanisms, may be differently influenced by alteration of the dipolar electric field of a lipid membrane. METHODS By using electrophysiological measurements on reconstituted lipid membranes, we used alamethicin, melittin and magainin to report on how controlled manipulation of the membrane(More)
The study of factors essential for protein-peptide interactions and protein pore-mediated peptide transport are of particular relevance in biology. Wild-type α-hemolysin was adopted as a "nanoreactor" in which perturbations of the current through a protein containing a lumen-residing, aryl-capped antimicrobial peptide were seen for the first time and(More)
TRPA1 is a nonselective cation channel activated by a wide variety of noxious chemicals. Intriguingly, several TRPA1 modulators induce a bimodal effect, activating the channel at micromolar concentrations and inhibiting it at higher concentrations. Here we report the bimodal action of cinnamaldehyde (CA) and camphor, which are thus far reported as agonist(More)
Little is known on antimicrobial peptide permeation through outer membrane channels in gram-negative bacteria. Herein, we probed at a single-molecule level the interaction of two different peptides, magainin 2 and HPA3P with OmpF from E. coli. HPA3P is an analogue of the antimicrobial peptide HP(2-20) isolated from the N-terminal region of the Helicobacter(More)
Single-nanopores have recently been used to electrically detect a wide range of analytes. Similarly, using electrophysiology, we demonstrate how a system comprised of an ion channel formed by α-hemolysin (α-HL) and single-cyclic γ-cyclodextrin (γ-CD) molecule permits the detection of, and differentiation between three different antibiotics from the β-lactam(More)
Herein we explored the role of topological distribution of aromatic amino acids in peptide-membrane interfacial interactions. The membrane activity of closely related peptides and their binding energy is sensitive to the positioning of minimum two tryptophans, and by the degree of flanking at the membrane interface mediated by aromatic amino acids.
We present herein a first proof of concept demonstrating the potential of a protein nanopore-based technique for real-time detection of selected Gram-negative bacteria (Pseudomonas aeruginosa or Escherichia coli) at a concentration of 1.2 × 108 cfu/mL. The anionic charge on the bacterial outer membrane promotes the electrophoretically driven migration of(More)
This work reports results of an atomic force microscopy (AFM) study of adhesion force between hydroxylated AFM tips and supported lipid bilayers (SLBs) of phosphatidylcholine in phosphate buffer saline solution at neutral pH. Silicon nitride AFM probes were hydroxylated by treatment in water vapor plasma and used in force spectroscopy measurements of(More)
Herein, we describe at uni-molecular level the interactions between poly(amidoamine) (PAMAM) dendrimers of generation 1 and the α-hemolysin protein nanopore, at acidic and neutral pH, and ionic strengths of 0.5 M and 1 M KCl, via single-molecule electrical recordings. The results indicate that kinetics of dendrimer-α-hemolysin reversible interactions is(More)