Combining multidimensional liquid chromatography and MALDI–TOF-MS for the fingerprint analysis of secreted peptides from the unexplored sea anemone species Phymanthus crucifer

Rodríguez, Armando A.; Ständker, Ludger; Zaharenko, André J.; Garateix, Anoland; Forssmann, Wolf‐Georg; Béress, L.; Valdés, Olga; Hernández, Yasnay; Laguna, Abilio

doi:10.1016/j.jchromb.2012.06.034

Cited by 13 publications

(8 citation statements)

References 90 publications

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“…Most of the ant venoms analysed have the majority of their peptides in the low molecular weight range (1-4 kDa). This suggests that ant venoms have peptides that are overall smaller than the peptidic component of other venomous animals such as scorpions (4-5 kDa) 68 , sea anemones (2-3.5 kDa) 69 and spiders (3-5 kDa and 6.5-8.5 kDa) 70 but not marine cone snails (0.5-3.5 kDa) 55 . However, formicoid ant venoms seem to be more complex than poneroid ant venoms and possess some larger peptides with masses up to 8 kDa.…”

Section: Maldi Matrix Optimisation Numerous Matrix Candidates Have Bmentioning

confidence: 99%

Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms

et al. 2016

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Animal venom peptides are currently being developed as novel drugs and bioinsecticides. Because ants use venoms for defense and predation, venomous ants represent an untapped source of potential bioactive toxins. This study compared the protein and peptide components of the poneroid ants Neoponera commutata, Neoponera apicalis, and Odontomachus hastatus and the formicoid ants Ectatomma tuberculatum, Ectatomma brunneum, and Myrmecia gulosa. 1D and 2D PAGE revealed venom proteins in the mass range <10 to >250 kDa. NanoLC-ESI-QTOF MS/MS analysis of tryptic peptides revealed the presence of common venom proteins and also many undescribed proteins. RP-HPLC separation followed by MALDI-TOF MS of the venom peptides also revealed considerable heterogeneity. It was found that the venoms contained between 144 and 1032 peptides with 5-95% of peptides in the ranges 1-4 and 1-8 kDa for poneroid and formicoid ants, respectively. By employing the reducing MALDI matrix 1,5-diaminonapthalene, up to 28 disulfide-bonded peptides were also identified in each of the venoms. In particular, the mass range of peptides from poneroid ants is lower than peptides from other venoms, indicating possible novel structures and pharmacologies. These results indicate that ant venoms represent an enormous, untapped source of novel therapeutic and bioinsecticide leads.

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Section: Maldi Matrix Optimisation Numerous Matrix Candidates Have Bmentioning

confidence: 99%

Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms

et al. 2016

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“…[8][9][10] However, as the venomous animal biodiversity encompasses ca 173 000 species, the vast majority of animal venoms remain unexplored in spite of their potential. Several large venomous animal groups have been little studied including centipedes, [11] ticks, [12] sea anemones, [13] wasps, [14] and ants. This is largely due to the small size and difficulty of collecting venoms or glands from these invertebrates.…”

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The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling

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Aili

et al. 2015

Rapid Comm Mass Spectrometry

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“…Proteomics and transcriptomics studies have shown that peptide diversity in sea anemone venoms is more complex than previously expected, indicating that a great number of new members of known classes and novel types of toxins remains unexplored [ 20 , 21 , 22 ]. Recently, we have structurally and functionally characterized two new members of sea anemone type 1 toxins, as well as a novel family (type 5) of K V -toxins, purified from the venom of B. caissarum population from Saint Peter and Saint Paul Archipelago, Brazil [ 16 , 23 ].…”

Section: Discussionmentioning

confidence: 99%

AbeTx1 Is a Novel Sea Anemone Toxin with a Dual Mechanism of Action on Shaker-Type K+ Channels Activation

et al. 2018

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Voltage-gated potassium (KV) channels regulate diverse physiological processes and are an important target for developing novel therapeutic approaches. Sea anemone (Cnidaria, Anthozoa) venoms comprise a highly complex mixture of peptide toxins with diverse and selective pharmacology on KV channels. From the nematocysts of the sea anemone Actinia bermudensis, a peptide that we named AbeTx1 was purified and functionally characterized on 12 different subtypes of KV channels (KV1.1–KV1.6; KV2.1; KV3.1; KV4.2; KV4.3; KV11.1; and, Shaker IR), and three voltage-gated sodium channel isoforms (NaV1.2, NaV1.4, and BgNaV). AbeTx1 was selective for Shaker-related K+ channels and is capable of inhibiting K+ currents, not only by blocking the K+ current of KV1.2 subtype, but by altering the energetics of activation of KV1.1 and KV1.6. Moreover, experiments using six synthetic alanine point-mutated analogs further showed that a ring of basic amino acids acts as a multipoint interaction for the binding of the toxin to the channel. The AbeTx1 primary sequence is composed of 17 amino acids with a high proportion of lysines and arginines, including two disulfide bridges (Cys1–Cys4 and Cys2–Cys3), and it is devoid of aromatic or aliphatic amino acids. Secondary structure analysis reveals that AbeTx1 has a highly flexible, random-coil-like conformation, but with a tendency of structuring in the beta sheet. Its overall structure is similar to open-ended cyclic peptides found on the scorpion κ-KTx toxins family, cone snail venoms, and antimicrobial peptides.

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Combining multidimensional liquid chromatography and MALDI–TOF-MS for the fingerprint analysis of secreted peptides from the unexplored sea anemone species Phymanthus crucifer

Cited by 13 publications

References 90 publications

Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms

Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms

The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling

AbeTx1 Is a Novel Sea Anemone Toxin with a Dual Mechanism of Action on Shaker-Type K+ Channels Activation

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