Natural products are well known for their biological relevance, high degree of three-dimensionality, and access to areas of largely unexplored chemical space. To shape our understanding of the interaction between natural products and protein targets in the postgenomic era, we have used native mass spectrometry to investigate 62 potential protein targets for malaria using a natural-product-based fragment library. We reveal here 96 low-molecular-weight natural products identified as binding partners of 32 of the putative malarial targets. Seventy-nine (79) fragments have direct growth inhibition on Plasmodium falciparum at concentrations that are promising for the development of fragment hits against these protein targets. This adds a fragment library to the published HTS active libraries in the public domain.

Excited states in 58,60,62 Ni were populated via inelastic proton scattering at the Australian National University as well as via inelastic neutron scattering at the University of Kentucky Accelerator Laboratory. The Super-e electron spectrometer and the CAESAR Compton-suppressed HPGe array were used in complementary experiments to measure conversion coefficients and δ(E2/M 1) mixing ratios, respectively, for a number of 2 + → 2 + transitions. The data obtained were combined with lifetimes and branching ratios to determine E0, M 1, and E2 transition strengths between 2 + states. The E0 transition strengths between 0 + states were measured using internal conversion electron spectroscopy and compare well to previous results from internal pair formation spectroscopy. The E0 transition strengths between the lowest-lying 2 + states were found to be consistently large for the isotopes studied.

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Social isolation appears to be negatively related to PA at the level of everyday life. Physical activity interventions with this population should consider including social components as a part of PA.

Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry (ESI-FTICR-MS or ESI-FTMS) was used to screen 192 natural product extracts and a 659-member natural product-based fragment library for bindings to a potential malaria drug target, Plasmodium falciparum Rab11a (PfRab11a, PF13_0119). One natural product extract and 11 fragments showed binding activity. A new natural product, arborside E, was identified from the active extract of Psydrax montigena as a weak binder. Its binding activity and inhibitory activity against PfRab11a were confirmed by ESI-FTMS titration experiments and an orthogonal enzyme assay.