A comparison of adhesive performance among six cursorial spider species

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  A comparison of adhesive performance among six cursorial spider species Abstract The ability to adhere to surfaces is particularly relevant for cursorial predatory arthropods like hunting spiders, which often traverse relatively complex environments characterized by large variation in substrate properties. Here, we evaluated the adhesive performance of six hunting spider species that are common in eastern temperate North America and lack specialized tarsi for climbing smooth or inclined surfaces [Lycosidae: Pardosa lapidicina Emerton, 1885 and Rabidosa rabida (Walckenaer, 1837); Oxyopidae: Oxyopes salticus Hentz, 1845; Pisauridae: Pisaurina mira (Walckenaer, 1837); Dolomedidae: Dolomedes triton (Walckenaer, 1837), and Dolomedes scriptus Hentz, 1845]. We tested adhesion performance as shear load resistance (g) on a glass plate, and as the angle of failure (°) when the plate was gradually inclined relative to horizontal. Average angle of failure and shear resistance differed among ...

Inhibitory effects of 6-O-palmitoyl-l-ascorbic acid (ASC16) on the enzymatic activity of Bothrops alternatus venom

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By Cláudio Timm - https://www.flickr.com/photos/cdtimm/4267955250/, CC BY-SA 2.0, https://commons.wikimedia.org/w/index.php?curid=13205355

Inhibitory effects of 6-O-palmitoyl-l-ascorbic acid (ASC16) on the enzymatic activity of Bothrops alternatus venom

Abstract

In the anti-venom production process, it is essential to use whole venom during immunization to generate specific antibodies capable of neutralizing all venom components. However, efforts are being made to improve the traditional immunization process by reducing the toxic effects of venom components on the immunized animals while ensuring an optimal immune response in accordance with good manufacturing practices. In this context, we aimed to evaluate the capacity of ASC16 to inhibit the enzymatic activity of the main components of B. alternatus venom. In vitro studies were conducted to evaluate the inhibitory effect of ASC16 on metalloproteinases (SVMP), serine proteinases (SVSP) and phospholipases A2 (PLA2) using specific substrates. In vivo assays measured edema-forming activity, and histological analysis with hematoxylin and eosin staining were performed. Additionally, hemorrhage inhibition was tested using a murine model. In silico studies were also carried out using bothropasin as a model. The results of enzyme inhibition showed that ASC16 significantly inhibited SVMP (49.31% ± 0.62), SVSP (63.11 ± 3.86%) and PLA2 activity (36.52% ± 0.09). ASC16 did not reduce edema but it significantly inhibited hemorrhage (66.32%). In silico analysis suggested that ASC16’s hydrophobic portion binds to critical residues involved in catalysis of the SVMP (Glu146 and His145), while the hydrophilic fraction also interacts with the protein (Pro109, Thr110, Gly112, and Tyr132). These findings position ASC16 as a promising candidate for use as an additive inhibitor in adjuvant formulations in antivenom immunization schemes for B. alternatus.

Maslovski, F., Pereañez, J.A., Hernández, D. et al. Inhibitory effects of 6-O-palmitoyl-l-ascorbic acid (ASC16) on the enzymatic activity of Bothrops alternatus venom. Arch Toxicol (2025). https://doi.org/10.1007/s00204-025-04188-9