What’s a Spider? Designation of the Neotype for the First Animal Species Ever Described, Araneus angulatus Clerck 1757 (Araneae: Araneidae)

  What’s a Spider? Designation of the Neotype for the First Animal Species Ever Described, Araneus angulatus Clerck 1757 (Araneae: Araneidae) Abstract We designate a neotype for the Eurasian spider species Araneus angulatus Clerck, 1757, thereby fixing the objective application of the species name, the genus name Araneus Clerck 1757, the family name Araneidae Clerck 1757, and the superfamily name Araneoidea Clerck 1757. By etymology and arachnological tradition, it also unofficially fixes the application of the ordinal name Araneae Clerck 1757 and thus answers the uncontroversial question, “What’s a spider?” A. angulatus also happens to be historically the first animal species ever described because Clerck (1757) has priority over Linnaeus (1758). Neotype designation is justified for three reasons: the syntypes of A. angulatus are lost; “ A. angulatus ” contains significant COI sequence divergence, potentially representing intraspecific variation, misidentifications, or as many...

Short-Chained Linear Scorpion Peptides: A Pool for Novel Antimicrobials

 


Short-Chained Linear Scorpion Peptides: A Pool for Novel Antimicrobials

Abstract

Scorpion venom peptides are generally classified into two main groups: the disulfide bridged peptides (DBPs), which usually target membrane-associated ion channels, and the non-disulfide bridged peptides (NDBPs), a smaller group with multifunctional properties. In the past decade, these peptides have gained interest because most of them display functions that include antimicrobial, anticancer, haemolytic, and anti-inflammatory activities. Our current study focuses on the short (9–19 amino acids) antimicrobial linear scorpion peptides. Most of these peptides display a net positive charge of 1 or 2, an isoelectric point at pH 9–10, a broad range of hydrophobicity, and a Grand Average of Hydropathy (GRAVY) Value ranging between −0.05 and 1.7. These features allow these peptides to be attracted toward the negatively charged phospholipid head groups of the lipid membranes of target cells, a force driven by electrostatic interactions. This review outlines the antimicrobial potential of short-chained linear scorpion venom peptides. Additionally, short linear scorpion peptides are in general more attractive for large-scale synthesis from a manufacturing point of view. The structural and functional diversity of these peptides represents a good starting point for the development of new peptide-based therapeutics.

Panayi, Tolis, Spiridoula Diavoli, Vicky Nicolaidou, Christos Papaneophytou, Christos Petrou, and Yiannis Sarigiannis. 2024. "Short-Chained Linear Scorpion Peptides: A Pool for Novel Antimicrobials" Antibiotics 13, no. 5: 422. https://doi.org/10.3390/antibiotics13050422