Functional characterization on invertebrate and vertebrate tissues of tachykinin peptides from octopus venoms |
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| Affiliation: | 1. Venom Evolution Laboratory, School of Biological Sciences, University of Queensland, St Lucia, Queensland 4072, Australia;2. School of Biomedical Sciences, University of Queensland, St Lucia, Queensland 4072, Australia;3. Department of Biological Science, Brock, Ontario, Canada L2S 3A1;4. Institute for Molecular Bioscience, University of Queensland, St Lucia, Queensland 4072, Australia;5. HEJ Research Institute of Chemistry, International Center for Chemical and Biological Sciences (ICCBS), University of Karachi, Karachi 75270, Pakistan;6. Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052, Australia;1. Division of Preclinical Research, Egis Pharmaceuticals PLC, Hungary;2. Chemical Research Division, Egis Pharmaceuticals PLC, Budapest, Hungary;3. MTA-SZTE Supramolecular and Nanostructured Materials Research Group of HAS, University of Szeged, Hungary;4. Department of Medical Chemistry, University of Szeged, Hungary;5. Institute of Pharmaceutical Analysis, SZTE-MTA Lendület Foldamer Research Group, University of Szeged, Szeged, Hungary;1. Department of Physics, Mathematics and Biophysics, Medical Academy, Lithuanian University of Health Sciences, Eiveniu 4, Kaunas LT 50161, Lithuania;2. Laboratory of Neurophysiology, Neuroscience Institute, Medical Academy, Lithuanian University of Health Sciences, Eiveniu 4, Kaunas LT 50161, Lithuania;1. Laboratory of Neuroscience, Department of Biophysics, Wrocław Medical University, Wrocław 50-368, Poland;2. Department of Molecular Physiology and Neurobiology, Wrocław University, Wrocław 50-335, Poland;1. Department of Hyginic chemistry, Meiji Pharmaceutical University, 2-522-1, Noshio, Kiyose-shi, Tokyo 204-8588, Japan;2. Meiji Pharmaceutical University, 2-522-1, Noshio, Kiyose-shi, Tokyo 204-8588, Japan;3. From the Medical Scientist Training Program and;4. the Departments of Neurology,;5. Pharmacology, and;12. Molecular Physiology and Biophysics, Vanderbilt University, Nashville, Tennessee 37240-7915,;6. the Veterans Affairs Tennessee Valley Healthcare System, Nashville, Tennessee 37212, and |
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| Abstract: | It has been previously shown that octopus venoms contain novel tachykinin peptides that despite being isolated from an invertebrate, contain the motifs characteristic of vertebrate tachykinin peptides rather than being more like conventional invertebrate tachykinin peptides. Therefore, in this study we examined the effect of three variants of octopus venom tachykinin peptides on invertebrate and vertebrate tissues. While there were differential potencies between the three peptides, their relative effects were uniquely consistent between invertebrate and vertebrae tissue assays. The most potent form (OCT-TK-III) was not only the most anionically charged but also was the most structurally stable. These results not only reveal that the interaction of tachykinin peptides is more complex than previous structure–function theories envisioned, but also reinforce the fundamental premise that animal venoms are rich resources of novel bioactive molecules, which are useful investigational ligands and some of which may be useful as lead compounds for drug design and development. |
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| Keywords: | Octopus Tachykinin Venom Peptide |
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