Novel structural class of four disulfide-bridged peptides from Tityus serrulatus venom

Pimenta, Adriano M.C.; Legros, Christian; Almeida, Flávia De Marco; Mansuelle, Pascal; Lima, Maria Elena de; Bougis, Pierre E.

doi:10.1016/s0006-291x(03)00082-2

Cited by 29 publications

(23 citation statements)

References 23 publications

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“…Biochemical characterization showed that they are 29 amino acids long, tightly reticulated by a new pattern of four disulphidebridges. These new molecules were classified as part of a novel structural class of short peptides, related to short K+ channels blockers from scorpion venoms (Pimenta et al, 2003b). However, in spite of a high homology in their Cterminal region with KTX1 and KTX2, which block K v 1.1 and K v 1.3 and are highly lethal to mice by i.c.v.…”

Section: Ts11 Ts12 Ts13 (Ts Peptides 1-3)mentioning

confidence: 99%

“…Sixteen residues could be aligned between these defensins and the 38 residues of the C-terminal part of the AaTX Kbeta, giving 42% sequence similarity (Legros et al, 1998). Latter, a screening achieved by MS on the toxic fractions obtained from molecular gel-filtration of the Tityus serrulatus venom allowed the purification and characterization of a truncated TsTX Kbeta (4081.76 Da) (Pimenta et al, 2003b). The Nterminal amino acids were cleaved after Lys 24 , giving a 36 amino acids toxin.…”

Section: Ts8 Previously Tstx Kbeta and Its Ortholog Ts19mentioning

confidence: 99%

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Potassium channel blockers from the venom of the Brazilian scorpion Tityus serrulatus ( )

Martin‐Eauclaire

Pimenta

Bougis

et al. 2016

Toxicon

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Section: Ts11 Ts12 Ts13 (Ts Peptides 1-3)mentioning

confidence: 99%

Section: Ts8 Previously Tstx Kbeta and Its Ortholog Ts19mentioning

confidence: 99%

Potassium channel blockers from the venom of the Brazilian scorpion Tityus serrulatus ( )

Martin‐Eauclaire

Pimenta

Bougis

et al. 2016

Toxicon

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“…We substituted the Val 26 for lysine and the Thr 24 for phenylalanine in PBTx1 corresponding to the conserved amino acid residues of the strong K ϩ channel blockers of subgroup 3 of the ␣-KTx scorpion toxins, like agitoxin 2. The substitutions indeed affect the binding of the rPBTx1 to the three Kv1-type channels; PBTx1 T24F/V26K displays a similar and strong increase in the affinity (10-fold increase).…”

Section: Discussionmentioning

confidence: 99%

“…In this mutant, the residues Thr 24 and Val 26 of PBTx1 were substituted by a phenylalanine and a lysine residue, respectively. In Fig.…”

Section: Physiological Effects Of the New Subfamily ␣-Ktx11mentioning

confidence: 99%

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A Subfamily of Acidic α-K+ Toxins

Huys

Olamendi-Portugal²,

García‐Gómez³

et al. 2004

Journal of Biological Chemistry

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Three homologous acidic peptides have been isolated from the venom of three different Parabuthus scorpion species, P. transvaalicus, P. villosus, and P. granulatus. Analysis of the primary sequences reveals that they structurally belong to subfamily 11 of short chain ␣-K ؉ -blocking peptides (Tytgat, J., Chandy, K. G., Garcia, M. L., Gutman, G. A., Martin-Eauclaire, M. F., van der Walt, J. J., and Possani, L. D. (1999) Trends Pharmacol. Sci. 20, 444 -447). These toxins are 36 -37 amino acids in length and have six aligned cysteine residues, but they differ substantially from the other ␣-K ؉ toxins because of the absence of the critical Lys 27 and their total overall negative charge. Parabutoxin 1 (PBTx1), which has been expressed by recombinant methods, has been submitted to functional characterization. Despite the lack of the Lys 27 , this toxin blocks several Kv1-type channels heterologously expressed in Xenopus oocytes but with low affinities (micromolar range). Because a relationship between the biological activity and the acidic residue substitutions may exist, we set out to elucidate the relative impact of the acidic character of the toxin and the lack of the critical Lys 27 on the weak activity of PBTx1 toward Kv1 channels. To achieve this, a specific mutant named rPBTx1 T24F/V26K was made recombinantly and fully characterized on Kv1-type channels heterologously expressed in Xenopus oocytes. Analysis of rPBTx1 T24F/V26K displaying an affinity toward Kv1.2 and Kv1.3 channels in the nanomolar range shows the importance of the functional dyad above the acidic character of this toxin.

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Small peptides, big world: biotechnological potential in neglected bioactive peptides from arthropod venoms

Pimenta

Lima

2005

Journal of Peptide Science

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Until recently, a toxinologist's tasks involved the search for highly toxic or lethal toxins in animal venoms that could explain the harmful effects in clinically observed symptoms. Most of these toxins were put on evidence using a function to structure approach, in which a biological phenomena observation usually guided the isolation and characterization of the causative molecule. Paving this way, many toxins were promptly purified because of their readily observed effect. Nevertheless, small molecules with micro-effects that are not easily visualized can be relatively neglected or poorly studied. This situation has changed now with the advent of the sensitivity, resolution and accuracy of techniques such as mass spectrometry and proteomic approaches used in toxinology. Taking advantage of these methodologies, small peptides with 'newly exploited' biological activities such as vasoactive, hormone-like, antimicrobial and others have been recently given much more attention, enlarging the known repertoire of bioactive molecules found in animal venoms. This article aims to review current knowledge on small biologically active peptides (<3 kDa) found in arthropod venoms and discuss their potentialities as new drug candidates or therapeutic lead compounds.

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Novel structural class of four disulfide-bridged peptides from Tityus serrulatus venom

Cited by 29 publications

References 23 publications

Potassium channel blockers from the venom of the Brazilian scorpion Tityus serrulatus ( )

Potassium channel blockers from the venom of the Brazilian scorpion Tityus serrulatus ( )

A Subfamily of Acidic α-K+ Toxins

Small peptides, big world: biotechnological potential in neglected bioactive peptides from arthropod venoms

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