An Overlooked Species of Enigmatic Wolf Spider (Araneae: Lycosidae) Clarifies the Mysterious Distribution of its Sibling

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  An Overlooked Species of Enigmatic Wolf Spider (Araneae: Lycosidae) Clarifies the Mysterious Distribution of its Sibling Abstract Several wolf spiders exhibit a peculiar geographical distribution. One good example of this is Pardosa aenigmatica Tongiorgi, 1966, recently recognized in Italy and the Middle East but missing in the Balkans. A comparison of populations from the disjunctive areas revealed that they would be better described as two distinct species. As a result, here we describe Pardosa sepidehae sp. nov. The paper includes detailed descriptions and comparative illustrations of male and female copulatory organs for the newly discovered species and P. aenigmatica. Pardosa sepidehae sp. nov. is distributed in the Middle East, whereas P. aenigmatica remains endemic to the Apennine Peninsula. Adile Akpinar, Petr Dolejš "An Overlooked Species of Enigmatic Wolf Spider (Araneae: Lycosidae) Clarifies the Mysterious Distribution of its Sibling," Annales Zoologici, 76(29), ...

Molecular Recognition and Immunopharmacological Implications of Serratiopeptidase Targeting Snake Venom Bradykinin-Potentiating Peptides

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Molecular Recognition and Immunopharmacological Implications of Serratiopeptidase Targeting Snake Venom Bradykinin-Potentiating Peptides

Abstract

Purpose

Bradykinin-potentiating peptides (BPPs), found in snake venom, are known to modulate cardiovascular functions, but their susceptibility to enzymatic degradation remains poorly understood.

Methods

Models were generated using AlphaFold-Colab for five small BPPs (< 9 amino acids) that did not have experimentally solved structures, and those BPPs which had reliable predictions of structure (pLDDT > 80) were used for docking studies. Protein-peptide docking experiments were done using HADDOCK for studying the interaction between wild-type (WT) and mutant serratiopeptidase with BPPs. After selecting the best complex, simulation of the complex was done using molecular dynamics (MD) simulations for 100 ns and binding energy determination using MM/PBSA analysis. For checking the mechanical stability of the protein-peptide complexes, Steered MD was performed.

Results

HADDOCK docking identified BPP-4 as a favorable binder of WT and mutant serratiopeptidase supported by a HADDOCK score of -109.1 ± 5.2 and minimal restraint violations. MD simulations revealed greater stability in the mutant complex supported by persistent hydrogen bonds, reduced RMSD/RMSF fluctuations, restricted conformational sampling in PCA, favorable MM/PBSA energy contributions, and a more stable conformational ensemble in cluster analysis. The Steered MD simulation showed a higher rupture force in the mutant BPP-4-serratiopeptidase complex compared to the WT.

Conclusions

Computational analysis identified BPP-4 as a promising serratiopeptidase-binding peptide, with differences in binding affinity and mechanical stability between WT and mutant complexes. The results offer insight into BPP-serratiopeptidase recognition at the molecular level and set the basis for future experiments on peptide binding.

Dhiman, A., Singh, R. & Purohit, R. Molecular Recognition and Immunopharmacological Implications of Serratiopeptidase Targeting Snake Venom Bradykinin-Potentiating Peptides. Pharm Res (2026). https://doi.org/10.1007/s11095-026-04222-0