In the picture: disulfide-poor conopeptides, a class of pharmacologically interesting compounds

 

Eline K. M. Lebbe¹, Jan Tytgat¹

 

1 Toxicology and Pharmacology, KU Leuven, O&N2, Box 922, Herestraat 49, 3000 Leuven, Belgium

 

ABSTRACT

During evolution, nature has embraced different strategies for species to survive. One strategy, applied by predators as diverse as snakes, scorpions, sea anemones and cone snails, is using venom to immobilize or kill a prey. This venom offers a unique and extensive source of chemical diversity as it is driven by the evolutionary pressure to improve prey capture and/or to protect their species. Cone snail venom is an example of the remarkable diversity in pharmacologically active small peptides that venoms can consist of. These venom peptides, called conopeptides, are classified into two main groups based on the number of cysteine residues, namely disulfide-rich and disulfide-poor conopeptides. Since disulfide-poor conotoxins are minor components of this venom cocktail, the number of identified peptides and the characterization of these peptides is far outclassed by its cysteine-rich equivalents. This review provides an overview of 12 families of disulfide-poor peptides identified to date as well as the state of affairs.

 

Keywords: Cone snail; Conopressin; Contryphan; Conantokin; Contulakin; Conorfamid; Conophan; Conomap; Conomarphin; Conolysin; ConoGAY; ConoCAP; Cono-NPY

 

Received: June 17, 2016.

Accepted: September 27, 2016.

 

Correspondence: jan.tytgat@kuleuven.be

 

Authors' contributions

EL wrote the first draft of the manuscript. JT revised the manuscript and provided financial support. Both authors read and approved the final manuscript.

 

Authors' information

EL is doctor in Pharmaceutical Sciences and MSc in Bioscience Engineering. JT is full professor at the faculty of Pharmaceutical Sciences, KU Leuven, Belgium.

 

Competing interests

The authors declare that they have no competing interests.

 

Consent for publication

Not applicable.