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. Author manuscript; available in PMC: 2023 May 9.
Published in final edited form as: Biochem Pharmacol. 2021 Jul 22;192:114693. doi: 10.1016/j.bcp.2021.114693

Fig. 2. Isolation of ponericins with anthelmintic activity from the venoms of N. apicalis and N. commutata.

Fig. 2.

Chromatograms showing analytical RP-HPLC fractionation of crude venom from (A) N. commutata and (D) N. apicalis, with peaks containing anthelmintic activity highlighted. Insets show N. commutata and N. apicalis worker ants (photographs by Dr Alex Wild, The University of Texas at Austin, USA). (B, C, E–G) Successive purification by analytical RP-HPLC identified five anthelmintic ponericins. Insets are MALDI TOF MS spectra showing the monoisotopic mass of each peptide. Amino acid sequences were determined using LC-MS/MS and compared against a draft venom-gland transcriptome for N. commutata and previously identified ponericins for N. apicalis. (H) An example mass spectrum showing ions leading to identification of the amino acid sequence for ponericin Nc2a.