Citation

Ruder T, Ali SA, Ormerod K, Brust A, Manchadi ML, Ventura S, Undheim EA, Jackson TN, Mercier AJ, King GF, Alewood PF, Fry BG. Peptides 2013; 47: 71-76.

Affiliation

Venom Evolution Laboratory, School of Biological Sciences, University of Queensland, St Lucia Queensland, 4072 Australia; School of Biomedical Sciences, University of Queensland, St Lucia Queensland, 4072 Australia.

Copyright

(Copyright © 2013, Elsevier Publishing)

DOI

10.1016/j.peptides.2013.07.002

PMID

23850991

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 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.

Language: en