G. Ferrat

Publications21
h-index12
Citations476
Highly Influential Citations18
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Induction of morphological changes in model lipid membranes and the mechanism of membrane disruption by a large scorpion-derived pore-forming peptide.
TLDR
Solid-state NMR results correlated well with the observed biological activity of pin1 in red blood cells and bacteria, and indicated that pin1(20-44) may be isotropically tumbling.
An unusual fold for potassium channel blockers: NMR structure of three toxins from the scorpion Opisthacanthus madagascariensis.
TLDR
It is demonstrated by electrophysiological experiments that Om-toxins decrease the amplitude of the K+ current of the rat channels Kv 1.1 and Kv1.2, as well as human KV1.3.
Evidence for Domain-specific Recognition of SK and Kv Channels by MTX and HsTx1 Scorpion Toxins*
TLDR
Data demonstrate that the helical region of MTX exerts a key role in SK channel recognition, whereas the β-sheet region of HsTx1 is crucial for activity on all other channel types tested.
Solution structure of hpTX2, a toxin from Heteropoda venatoria spider that blocks Kv4.2 potassium channel.
TLDR
The high density in aromatic side chains of the putative functional surface as well as the lack of an asparagine is proposed to be the structural basis of the specificity of HpTX2 toward Kv4.2 potassium channel.
Chemical synthesis and structure-activity relationships of Ts kappa, a novel scorpion toxin acting on apamin-sensitive SK channel.
TLDR
Data from binding assay, together with conformational analysis of the synthetic analogues by 1H-NMR, suggest that Arg6, and to a lesser extent Arg9, are important residues for an high-affinity interaction of this toxin with SK channels; interestingly these residues are located outside thealpha-helical structure, whereas the pharmacologically important basic residues from other SK channel-specific toxins had been located inside the alpha-helix.
Solution structure of two insect‐specific spider toxins and their pharmacological interaction with the insect voltage‐gated Na+ channel
TLDR
The structure and the electrostatic anisotropy of those peptides to other sodium and calcium channel toxins are compared, and it is concluded that the recognition of insect voltage‐gated sodium channels by these toxins involves the β‐sheet, in addition to loops I and IV.
Induced refolding of a temperature denatured llama heavy‐chain antibody fragment by its antigen
TLDR
The results suggest an induced refolding of denatured VHH‐R2 by its antigen under these extreme conditions, and showed some similarities with the well established “induced fit” mechanism of antibody–antigen interactions at ambient temperature.
Solution structure of Phrixotoxin 1, a specific peptide inhibitor of Kv4 potassium channels from the venom of the theraphosid spider Phrixotrichus auratus
TLDR
This work has solved the solution structure of Phrixotoxin 1, a gating modifier of Kv4 potassium channels and proposed a toxin interacting surface that encompasses both the surface from which the dipole moment emerges and a neighboring hydrophobic surface rich in aromatic residues.
Synthesis, 1H NMR Structure, and Activity of a Three-disulfide-bridged Maurotoxin Analog Designed to Restore the Consensus Motif of Scorpion Toxins*
TLDR
An MTX analog with three instead of four disulfide bridges is designed and chemically synthesized and the entire consensus motif of scorpion toxins was restored by the substitution of the two half-cystines in positions 19 and 34 by two isosteric α-aminobutyrate (Abu) derivatives.
Selective inhibition of trypsins by insect peptides: role of P6-P10 loop.
TLDR
This work represents a first attempt in tuning the selectivity of natural peptidic serine protease inhibitors by mutating residues out of the reactive loop (P3-P'3).
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