Wandering spiders (family Ctenidae) have multicomponent venoms in which more than500 different peptides and proteins, called ctenitoxins, have been identified. The maincomponents of the venom are cysteine-rich peptides containing an inhibitory cystine knot(ICK) motif. The pharmacological diversity of ctenitoxins allows us to consider some of themas prototypes for the development of new drugs for the treatment of chronic pain,Huntington’s disease, erectile dysfunction and glaucoma. According to the location ofcysteine residues in the amino acid sequence, ctenitoxins are divided into 14 groupscontaining from 6 to 14 Cys residues. Currently, the spatial structure of only one ctenitoxin,ω-CNTX-Pn4a (Pha1β or Tx3-6) from the Brazilian wandering spider Phoneutria nigriventer,has been determined. Another 10 structural groups of ctenitoxins have homology with theknown spatial structures of spider toxins of other families and other proteins, and for threegroups the structural homologues are unknown. In this paper, we proposed possible disulfidebonding patterns for all groups of ctenitoxins. A comparison of the obtained schemes with thepredictions of the AlphaFold 2.0 program shows that this neural network does not alwayscorrectly predict the structures of cysteine-rich peptides, especially if the structures of maturemolecules without leader sequences are modeled.