Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator

Corzo, Gerardo; Escoubas, Pierre; Villegas, Elba; Barnham, Kevin J.; He, Weilan; Norton, Raymond S.; Nakajima, Terumi

doi:10.1042/0264-6021:3590035

Cited by 104 publications

(68 citation statements)

References 49 publications

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“…Different peptides reported in scorpion venoms show an amphipathic α-helical structure, like those reported for different cationic antimicrobial molecules [15,16,17,18,19,20,21,22,23]. These peptides, show hemolytic, immune modulating, antibacterial, and insecticidal activities [1,23,24].…”

Section: Introductionmentioning

confidence: 96%

Intraspecific Variation of Centruroides Edwardsii Venom from Two Regions of Colombia

Estrada-Gómez

Cupitra

Arango

et al. 2014

Toxins

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We report the first description studies, partial characterization, and intraspecific difference of Centruroides edwardsii, Gervais 1843, venom. C. edwardsii from two Colombian regions (Antioquia and Tolima) were evaluated. Both venoms showed hemolytic activity, possibly dependent of enzymatic active phospholipases, and neither coagulant nor proteolytic activities were observed. Venom electrophoretic profile showed significant differences between C. edwardsii venom from both regions. A high concentration of proteins with molecular masses between 31 kDa and 97.4 kDa, and an important concentration close or below 14.4 kDa were detected. RP-HPLC retention times between 38.2 min and 42.1 min, showed bands close to 14.4 kDa, which may correspond to phospholipases. RP-HPLC venom profile showed a well conserved region in both venoms between 7 and 17 min, after this, significant differences were detected. From Tolima region venom, 50 well-defined peaks were detected, while in the Antioquia region venom, 55 well-defined peaks were detected. Larvicidal activity was only detected in the C. edwardsii venom from Antioquia. No antimicrobial activity was observed using complete venom or RP-HPLC collected fractions of both venoms. Lethally activity (carried out on female albino swiss mice) was detected at doses over 19.2 mg/kg of crude venom. Toxic effects included distress, excitability, eye irritation and secretions, hyperventilation, ataxia, paralysis, and salivation.

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Section: Introductionmentioning

confidence: 96%

Intraspecific Variation of Centruroides Edwardsii Venom from Two Regions of Colombia

Estrada-Gómez

Cupitra

Arango

et al. 2014

Toxins

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“…High-resolution structure of Pin2, determined by NMR, showed that the peptide is essentially alpha-helical with a proline, which induces a structural “ kink ” in the central part of its structure [15]. The proline “ kink ” is a structural characteristic of some CAMPs that confer them high pore-forming abilities.…”

Section: Introductionmentioning

confidence: 99%

Characterization of Antibacterial and Hemolytic Activity of Synthetic Pandinin 2 Variants and Their Inhibition against Mycobacterium tuberculosis

et al. 2014

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The contention and treatment of Mycobacterium tuberculosis and other bacteria that cause infectious diseases require the use of new type of antibiotics. Pandinin 2 (Pin2) is a scorpion venom antimicrobial peptide highly hemolytic that has a central proline residue. This residue forms a structural “kink” linked to its pore-forming activity towards human erythrocytes. In this work, the residue Pro14 of Pin2 was both substituted and flanked using glycine residues (P14G and P14GPG) based on the low hemolytic activities of antimicrobial peptides with structural motifs Gly and GlyProGly such as magainin 2 and ponericin G1, respectively. The two Pin2 variants showed antimicrobial activity against E. coli, S. aureus, and M. tuberculosis. However, Pin2 [GPG] was less hemolytic (30%) than that of Pin2 [G] variant. In addition, based on the primary structure of Pin2 [G] and Pin2 [GPG], two short peptide variants were designed and chemically synthesized keeping attention to their physicochemical properties such as hydrophobicity and propensity to adopt alpha-helical conformations. The aim to design these two short antimicrobial peptides was to avoid the drawback cost associated to the synthesis of peptides with large sequences. The short Pin2 variants named Pin2 [14] and Pin2 [17] showed antibiotic activity against E. coli and M. tuberculosis. Besides, Pin2 [14] presented only 25% of hemolysis toward human erythrocytes at concentrations as high as 100 µM, while the peptide Pin2 [17] did not show any hemolytic effect at the same concentration. Furthermore, these short antimicrobial peptides had better activity at molar concentrations against multidrug resistance M. tuberculosis than that of the conventional antibiotics ethambutol, isoniazid and rifampicin. Therefore, Pin2 [14] and Pin2 [17] have the potential to be used as an alternative antibiotics and anti-tuberculosis agents with reduced hemolytic effects.

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“…Scorpion venom has been investigated mostly for its neurotoxins acting on different ion channels [1][2][3]. Recently, a-helical pore-forming peptides have been discovered in scorpion venom (parabutoporin [4], hadrurin [5], IsCTs [6,7] and pandinins [8]). In addition, the cDNA sequence of a peptide from Buthus martensii has been described, but biological activity of the peptide has not yet been studied [9].…”

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confidence: 99%

Antibacterial and antifungal properties of α‐helical, cationic peptides in the venom of scorpions from southern Africa

Moerman

Bosteels

Noppe

et al. 2002

European Journal of Biochemistry

155

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Two novel pore-forming peptides have been isolated from the venom of the South-African scorpion Opistophtalmus carinatus. These peptides, designated opistoporin 1 and 2, differ by only one amino acid and belong to a group of a-helical, cationic peptides. For the first time, a comparison of the primary structures of a-helical pore-forming peptides from scorpion venom was undertaken. This analysis revealed that peptides in the range of 40-50 amino acids contain a typical scorpion conserved sequence S(x) 3 KxWxS(x) 5 L. An extensive study of biological activity of synthesized opistoporin 1 and parabutoporin, a poreforming peptide previously isolated from the venom of the South-African scorpion Parabuthus schlechteri, was undertaken to investigate an eventual cell-selective effect of the peptides. Opistoporin 1 and parabutoporin were most active in inhibiting growth of Gram-negative bacteria (1.3-25 lM), while melittin and mastoparan, two well-known cytolytic peptides, were more effective against Gram-positive bacteria in the same concentration range. In addition, the peptides showed synergistic activity with some antibiotics commonly used in therapy. Opistoporin 1 and parabutoporin had hemolytic activity intermediate between the least potent mastoparan and the highly lytic melittin. Furthermore, all peptides inhibited growth of fungi. Experiments with SYTOX green suggested that this effect is related to membrane permeabilization.

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Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator

Cited by 104 publications

References 49 publications

Intraspecific Variation of Centruroides Edwardsii Venom from Two Regions of Colombia

Intraspecific Variation of Centruroides Edwardsii Venom from Two Regions of Colombia

Characterization of Antibacterial and Hemolytic Activity of Synthetic Pandinin 2 Variants and Their Inhibition against Mycobacterium tuberculosis

Antibacterial and antifungal properties of α‐helical, cationic peptides in the venom of scorpions from southern Africa

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