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Enjoy your content with Smart Hub and One Remote Control. Welcome to the New Home Discover how you can make your life easier and more convenient. †‡ §∥⊥ DOI: *Phone: . E-mail: Graham.Nicholson@uts.edu.au.AbstractAnimal venom peptides are currently being developed as novel drugs and bioinsecticides. Because ants use venoms for defense and predation, venomous ants represent an untapped source of potential bioactive toxins. This study compared the protein and peptide components of the poneroid ants Neoponera commutata, Neoponera apicalis, and Odontomachus hastatus and the formicoid ants Ectatomma tuberculatum, Ectatomma brunneum, and Myrmecia gulosa. 1D and 2D PAGE revealed venom proteins in the mass range <10 to >250 kDa. NanoLC-ESI-QTOF MS/MS analysis of tryptic peptides revealed the presence of common venom proteins and also many undescribed proteins. RP-HPLC separation followed by MALDI-TOF MS of the venom peptides also revealed considerable heterogeneity. It was found that the venoms contained between 144 and 1032 peptides with 5–95% of peptides in the ranges 1–4 and 1–8 kDa for poneroid and formicoid ants, respectively.

By employing the reducing MALDI matrix 1,5-diaminonapthalene, up to 28 disulfide-bonded peptides were also identified in each of the venoms. In particular, the mass range of peptides from poneroid ants is lower than peptides from other venoms, indicating possible novel structures and pharmacologies. These results indicate that ant venoms represent an enormous, untapped source of novel therapeutic and bioinsecticide leads.Keywords: ant venomHymenopteraLC-MALDI-TOF MSmass spectrometrynanoLC-ESI-QTOF MS/MSpeptidomeproteomic analysistoxin Supporting InformationThe Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.jproteome.6b00182.Methodology for the identification of disulfide-bonded peptides as well as annotated spectra from 2D gel spots where a protein was identified from a single peptide. View: ACS ActiveView PDF | DOI: *E-mail: mwinnik@chem.utoronto.ca.AbstractIsothermal titration calorimetry (ITC) is a technique to measure the stoichiometry and thermodynamics from binding experiments.

Identifying an appropriate mathematical model to evaluate titration curves of receptors with multiple sites is challenging, particularly when the stoichiometry or binding mechanism is not available. In a recent theoretical study, we presented a differential binding model (DBM) to study calorimetry titrations independently of the interaction among the binding sites (Herrera, I.; Winnik, M. A. J. Phys. Chem. B 2013, 117, 8659–8672). Here, we build upon our DBM and show its practical application to evaluate calorimetry titrations of receptors with multiple sites independently of the titration direction. ecoquest flair air purifier reviewsSpecifically, we present a set of ordinary differential equations (ODEs) with the general form d[S]/dV that can be integrated numerically to calculate the equilibrium concentrations of free and bound species S at every injection step and, subsequently, to evaluate the volume-normalized heat signal (δQV = δq/dV) of direct and reverse calorimetry titrations. homedics hepa air cleaner ar20