Spider venoms are complex mixtures containing neuropeptides that act on ion channels and neurotransmitter receptors. In this study, we investigated Ap1a and Ap1b, two homologous peptides isolated from the venom of the Brazilian tarantula Acanthoscurria paulensis. Ap1a, the most abundant peptide in this venom, and Ap1b, its isoform differing by a single hydrophobic residue (Ile42 → Val), were classified within the Huwentoxin-II family and exhibit structural features consistent with the inhibitor cystine knot (ICK) motif.

Spider venoms are complex mixtures containing neuropeptides that act on ion channels and neurotransmitter receptors. In this study, we investigated Ap1a and Ap1b, two homologous peptides isolated from the venom of the Brazilian tarantula Acanthoscurria paulensis. Ap1a, the most abundant peptide in this venom, and Ap1b, its isoform differing by a single hydrophobic residue (Ile42 → Val), were classified within the Huwentoxin-II family and exhibit structural features consistent with the inhibitor cystine knot (ICK) motif.

Ao extrair uma molécula do sangue da aranha Acanthoscurria rondoniae, cientistas do Instituto Butantan identificaram uma possível terapia contra fungos resistentes. Em testes, a substância conseguiu combater fungos do gênero Candida e Trichosporon. Batizada de rondonina, a molécula teve ação específica contra os patógenos, indicando baixo risco de toxicidade para humanos. O animal é uma espécie de tarântula da Amazônia.