Kbot55, purified from Buthus occitanus tunetanus venom, represents the first member of a novel α-KTx subfamily

ElFessi-Magouri, Rym; Peigneur, Steve; Khamessi, Oussema; Srairi-Abid, Najet; Elayeb, Mohamed; Mille, Bea G.; Cuypers, Eva; Tytgat, Jan; Kharrat, Riadh

doi:10.1016/j.peptides.2015.05.015

Cited by 7 publications

(7 citation statements)

References 26 publications

(27 reference statements)

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“…Different fractions were eluted and tested for their toxicity on mice. Only a fraction (BotG50) showing a toxic activity [28][29] was then applied onto semi preparative reversed-phase HPLC C8 column (10 mm x 250mm, 5 μm, Beckman Fullerton) equilibrated in 0.1% trifluoroacetic acid in water, at a flow rate of 1ml/min. HPLC purification of the non-retained fraction was performed using an analytical C18 reversed-phase HPLC column (4.6mm…”

Section: Purification Of Rkmentioning

confidence: 99%

“…Reduction and alkylation of peptides and sequence determination of native and S-alkylated peptide were performed as described by Khammessi et al [27][28][29][30]…”

Section: Amino Acid Sequence Determination and Peptide Synthesismentioning

confidence: 99%

“…RK was substantially purified from the Buthus occitanus tunetanus scorpion venom by a first stage of gel filtration on a Sephadex G-50 column chromatography as previously described [29]. The toxic fraction (BotG50) obtained from this separation was purified by high performance liquid chromatography (HPLC) using a semi preparative C8 column.…”

Section: Purification Of the Peptidementioning

confidence: 99%

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RK, the first scorpion peptide with dual disintegrin activity on α1β1 and αvβ3 integrins

Khamessi

Mabrouk

Othman

et al. 2018

International Journal of Biological Macromolecules

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the first scorpion peptide with dual disintegrin activity on α1β1 and αvβ3 integrins. Abstract:Scorpion peptides are well known for their pharmaceutical potential on different targets. These include mainly the ion channels which were found to be highly expressed in many diseases, including cancer, auto-immune pathologies and Alzheimer. So far, however, the disintegrin activity had only been characterized for snake venom molecules. Herein, we present the first short peptide, purified from the venom of Buthus occitanus tunetanus, (termed RK) able to inhibit the cell adhesion of Glioblastoma, Melanoma and Rat pheochromocytoma to different extracellular matrix (ECM) receptors. Anti-integrin antibody assay suggests that RK interacts with both α1β1 and αvβ3 with a more pronounced effect for the former. The examination of the primary structure of RK suggests the involvement of two motifs: KSS, analogue to KTS which was characterized for α1β1 Snake venom disintegrins, and ECD, analogue to RGD which was found to be active on αvβ3. To assess their roles in the disintegrin activity of RK, we conducted a computational analysis. The molecular docking study shows that RK involves mainly two segments to interact with the α1β1 integrin, but the peptide does not implicate the KSS motif in the interaction. The molecular modeling study, suggests the key contribution of the ECD segment in the interaction with αvβ3 integrin.

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Section: Purification Of Rkmentioning

confidence: 99%

“…Reduction and alkylation of peptides and sequence determination of native and S-alkylated peptide were performed as described by Khammessi et al [27][28][29][30]…”

Section: Amino Acid Sequence Determination and Peptide Synthesismentioning

confidence: 99%

Section: Purification Of the Peptidementioning

confidence: 99%

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RK, the first scorpion peptide with dual disintegrin activity on α1β1 and αvβ3 integrins

Khamessi

Mabrouk

Othman

et al. 2018

International Journal of Biological Macromolecules

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“…Of these the aeKTx family is the largest, consisting of 30 subfamilies, and can either block ion conduction in Kv1, KCa2, and KCa3 channels via intrusion of a conserved essential dyad, a paired lysine and aromatic residue, into the channel selectivity filter, or by binding to the negatively charged extracellular loop of the KCa2 channel (Tytgat et al, 1999;Quintero-Hernandez et al, 2013;Dutertre and Lewis, 2010;Nirthanan et al, 2005;Rodriguez de la Vega and. Possani, 2004).…”

Section: Overview Of Sctx Actions On Potassium Channelsmentioning

confidence: 99%

Scorpion toxin peptide action at the ion channel subunit level

Housley

Liddell

et al. 2017

Neuropharmacology

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a b s t r a c tThis review categorizes functionally validated actions of defined scorpion toxin (SCTX) neuropeptides across ion channel subclasses, highlighting key trends in this rapidly evolving field. Scorpion envenomation is a common event in many tropical and subtropical countries, with neuropharmacological actions, particularly autonomic nervous system modulation, causing significant mortality. The primary active agents within scorpion venoms are a diverse group of small neuropeptides that elicit specific potent actions across a wide range of ion channel classes. The identification and functional characterisation of these SCTX peptides has tremendous potential for development of novel pharmaceuticals that advance knowledge of ion channels and establish lead compounds for treatment of excitable tissue disorders. This review delineates the unique specificities of 320 individual SCTX peptides that collectively act on 41 ion channel subclasses. Thus the SCTX research field has significant translational implications for pathophysiology spanning neurotransmission, neurohumoral signalling, sensori-motor systems and excitation-contraction coupling.This article is part of the Special Issue entitled 'Venom-derived Peptides as Pharmacological Tools.'

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“…Alpha-KTx toxins form the largest KTx family, and 31 subfamilies have been described [ 6 ]. They are short-chain peptides of 23 to 42 amino acid residues, cross-linked by three to four disulfide bridges [ 7 ].…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of Bot33: A Non-Toxic Peptide from the Venom of Buthus occitanus tunetanus Scorpion

et al. 2022

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Scorpion venom is a rich source of promising therapeutic compounds, such as highly selective ion channel ligands with potent pharmacological effects. Bot33 is a new short polypeptide of 38 amino acid residues with six cysteines purified from the venom of the Buthus occitanus tunetanus scorpion. Bot33 has revealed less than 40% identity with other known alpha-KTx families. This peptide displayed a neutral amino acid (Leucine), in the position equivalent to lysine 27, described as essential for the interaction with Kv channels. Bot33 did not show any toxicity following i.c.v. injection until 2 µg/kg mouse body weight. Due to its very low venom concentration (0.24%), Bot33 was chemically synthesized. Unexpectedly, this peptide has been subjected to a screening on ion channels expressed in Xenopus laevis oocytes, and it was found that Bot33 has no effect on seven Kv channel subtypes. Interestingly, an in silico molecular docking study shows that the Leu27 prevents the interaction of Bot33 with the Kv1.3 channel. All our results indicate that Bot33 may have a different mode of action from other scorpion toxins, which will be interesting to elucidate.

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Kbot55, purified from Buthus occitanus tunetanus venom, represents the first member of a novel α-KTx subfamily

Cited by 7 publications

References 26 publications

RK, the first scorpion peptide with dual disintegrin activity on α1β1 and αvβ3 integrins

RK, the first scorpion peptide with dual disintegrin activity on α1β1 and αvβ3 integrins

Scorpion toxin peptide action at the ion channel subunit level

Purification and Characterization of Bot33: A Non-Toxic Peptide from the Venom of Buthus occitanus tunetanus Scorpion

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