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...

The genome sequence of the spider, Parasteatoda lunata (Clerck, 1757)

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The genome sequence of the spider, Parasteatoda lunata (Clerck, 1757)

Abstract

We present a genome assembly from an individual female Parasteatoda lunata (spider; Arthropoda; Arachnida; Araneae; Theridiidae). The genome sequence is 1,411.4 megabases in span. Most of the assembly is scaffolded into 12 chromosomal, including the X1 and X2 sex chromosomes. The mitochondrial genome has also been assembled and is 14.29 kilobases in length.


Oxford G, Natural History Museum Genome Acquisition Lab, Darwin Tree of Life Barcoding collective et al. The genome sequence of the spider, Parasteatoda lunata (Clerck, 1757) [version 1; peer review: 3 approved]. Wellcome Open Res 2023, 8:271 (https://doi.org/10.12688/wellcomeopenres.19585.1)