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Abstract: Sea anemones are known to contain a wide diversity of biologically active peptides, mostly unexplored according to recent peptidomic and transcriptomic studies. In the present work, the neurotoxic fractions from the exudates of Stichodactyla helianthus and Bunodosoma granulifera were analyzed by reversed-phase chromatography and mass spectrometry. The first peptide fingerprints of these sea anemones were assessed, revealing the largest number of peptide components (156) so far found in sea anemone species, as well as the richer peptide diversity of B. granulifera in relation to S. helianthus. The transcriptomic analysis of B. granulifera, performed by massive cDNA sequencing with 454 pyrosequencing approach allowed the discovery of five new APETx-like peptides (U-AITX-Bg1a–e – including the full sequences of their precursors for four of them), which together with type 1 sea anemone sodium channel toxins constitute a very distinguishable feature of studied sea anemone species belonging to genus Bunodosoma. The molecular modeling of these new APETx-like peptides showed a distribution of positively charged and aromatic residues in putative contact surfaces as observed in other animal toxins. On the other hand, they also showed variable electrostatic potentials, thus suggesting a docking onto their targeted channels in different spatial orientations. Moreover several crab paralyzing toxins (other than U-AITX-Bg1a–e), which induce a variety of symptoms in crabs, were isolated. Some of them presumably belong to new classes of crab-paralyzing peptide toxins, especially those with molecular masses below 2kDa, which represent the smallest peptide toxins found in sea anemones. [Copyright &y& Elsevier]

Abstract: Food traceability is essential to preserve the identity of unique quality traits against frauds or commercial disputes. Therefore, there is a growing demand of new traceability systems for the collection of information related to units/batches of food ingredients and products. A rapid method based on peptide profiles obtained from tryptic digests of whole wine proteins by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry is described. Reliable peptide fingerprints were obtained for high quality Campania white wines, providing a signature of the finished products. The MALDI spectra revealed the presence of common diagnostic ions, but also evidenced differences between wines. Furthermore, the MALDI-TOF spectral traces were converted into simulated images to obtain a graphical representation of spectra. The resulting “mass codes” constitute a simple tool to display differences between samples, suggesting their potential use as “biological bar codes” for food authenticity and traceability, probably applicable to other classes of certified food products. [Copyright &y& Elsevier]