Spatial Scale Modulates the Effect of Habitat Amount on Diversity Patterns of Arachnid Assemblages Across Different Brazilian Ecosystems

  Spatial Scale Modulates the Effect of Habitat Amount on Diversity Patterns of Arachnid Assemblages Across Different Brazilian Ecosystems ABSTRACT Aim We evaluated how native vegetation cover influences the diversity of arachnid assemblages across multiple spatial scales in major Brazilian ecosystems. Location Brazil (Amazon and Atlantic rainforests, Cerrado savanna and Caatinga dry forest). Taxon Arachnida (Opiliones, Pseudoscorpiones and Scorpiones). Methods We sampled arachnids at 120 sites using active search and litter sifting. Native vegetation cover was quantified at three spatial scales (100, 200 and 300 m buffers) using GIS data. Assemblage structure was assessed using abundance, species richness, and Hill numbers ( q  = 0, 1 and 2). Generalized linear mixed models were used to evaluate responses across taxonomic groups and ecosystems. Results We recorded 3986 individuals from 179 species. Diversity responses to native vegetation cover were taxon-, ecosystem- and scale-de...

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