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Heus F, Otvos RA, Aspers RL, et al. Miniaturized bioaffinity assessment coupled to mass spectrometry for guided purification of bioactives from toad and cone snail. Biology (Basel). 2014;3(1):139-56doi: 10.3390/biology3010139.
Heus, F., Otvos, R. A., Aspers, R. L., van Elk, R., Halff, J. I., Ehlers, A. W., Dutertre, S., Lewis, R. J., Wijmenga, S., Smit, A. B., Niessen, W. M., & Kool, J. (2014). Miniaturized bioaffinity assessment coupled to mass spectrometry for guided purification of bioactives from toad and cone snail. Biology, 3(1), 139-56. https://doi.org/10.3390/biology3010139
Heus, Ferry, et al. "Miniaturized bioaffinity assessment coupled to mass spectrometry for guided purification of bioactives from toad and cone snail." Biology vol. 3,1 (2014): 139-56. doi: https://doi.org/10.3390/biology3010139
Heus F, Otvos RA, Aspers RL, van Elk R, Halff JI, Ehlers AW, Dutertre S, Lewis RJ, Wijmenga S, Smit AB, Niessen WM, Kool J. Miniaturized bioaffinity assessment coupled to mass spectrometry for guided purification of bioactives from toad and cone snail. Biology (Basel). 2014 Feb 13;3(1):139-56. doi: 10.3390/biology3010139. PMID: 24833338; PMCID: PMC4009767.
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Biology (Basel). 2014 Feb 13;3(1):139-56. doi: 10.3390/biology3010139.

Miniaturized bioaffinity assessment coupled to mass spectrometry for guided purification of bioactives from toad and cone snail.

Biology

Ferry Heus, Reka A Otvos, Ruud L E G Aspers, Rene van Elk, Jenny I Halff, Andreas W Ehlers, Sébastien Dutertre, Richard J Lewis, Sybren Wijmenga, August B Smit, Wilfried M A Niessen, Jeroen Kool

Affiliations

  1. AIMMS Division of BioMolecular Analysis, Faculty of Sciences, VU University Amsterdam, De Boelelaan 1081, 1083 HV Amsterdam, The Netherlands. [email protected].
  2. AIMMS Division of BioMolecular Analysis, Faculty of Sciences, VU University Amsterdam, De Boelelaan 1081, 1083 HV Amsterdam, The Netherlands. [email protected].
  3. Department of Biophysical Chemistry, Institute for Molecules and Materials, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. [email protected].
  4. Department of Molecular and Cellular Neurobiology, Center for Neurogenomics and Cognitive Research, Neuroscience Campus Amsterdam, VU University Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands. [email protected].
  5. AIMMS Division of BioMolecular Analysis, Faculty of Sciences, VU University Amsterdam, De Boelelaan 1081, 1083 HV Amsterdam, The Netherlands. [email protected].
  6. AIMMS Division of Organic Chemistry, Faculty of Sciences, VU University Amsterdam, De Boelelaan 1081, 1083 HV Amsterdam, The Netherlands. [email protected].
  7. The Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland 4072, Australia. [email protected].
  8. The Institute for Molecular Bioscience, The University of Queensland, St Lucia, Queensland 4072, Australia. [email protected].
  9. Department of Biophysical Chemistry, Institute for Molecules and Materials, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. [email protected].
  10. Department of Molecular and Cellular Neurobiology, Center for Neurogenomics and Cognitive Research, Neuroscience Campus Amsterdam, VU University Amsterdam, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands. [email protected].
  11. AIMMS Division of BioMolecular Analysis, Faculty of Sciences, VU University Amsterdam, De Boelelaan 1081, 1083 HV Amsterdam, The Netherlands. [email protected].
  12. AIMMS Division of BioMolecular Analysis, Faculty of Sciences, VU University Amsterdam, De Boelelaan 1081, 1083 HV Amsterdam, The Netherlands. [email protected].

PMID: 24833338 PMCID: PMC4009767 DOI: 10.3390/biology3010139

Abstract

A nano-flow high-resolution screening platform, featuring a parallel chip-based microfluidic bioassay and mass spectrometry coupled to nano-liquid chromatography, was applied to screen animal venoms for nicotinic acetylcholine receptor like (nAChR) affinity by using the acetylcholine binding protein, a mimic of the nAChR. The potential of this microfluidic platform is demonstrated by profiling the Conus textile venom proteome, consisting of over 1,000 peptides. Within one analysis (<90 min, 500 ng venom injected), ligands are detected and identified. To show applicability for non-peptides, small molecular ligands such as steroidal ligands were identified in skin secretions from two toad species (Bufo alvarius and Bufo marinus). Bioactives from the toad samples were subsequently isolated by MS-guided fractionation. The fractions analyzed by NMR and a radioligand binding assay with α7-nAChR confirmed the identity and bioactivity of several new ligands.

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