ARS | Publication request: Sulfakinins

Submitted to: Handbook of Biologically Active Peptides
Publication Type: Book / Chapter
Publication Acceptance Date: December 28, 2011
Publication Date: N/A

Interpretive Summary: Insect pests have developed resistance to several conventional pesticides, and new approaches are needed for pest management. Although neuropeptides (short chains of amino acids) serve as potent messengers in insects to regulate vital functions, the neuropeptides hold little promise as pest control agents because they can be degraded in the target pest. New, selective control agents may be developed by designing mimics of these neuropeptides that resist degradation and either inhibit or over-stimulate critical neuropeptide-regulated life functions. This book chapter represents a review of neuropeptides of the ‘sulfakinin’ class that control muscle-contraction, food-intake inhibition, and digestive enzyme release in insects. Structural studies have shed light on how sulfakinin peptides interact with the active site. The discoveries reviewed in this chapter will aid in the design of neuropeptide-like compounds capable of disrupting both the feeding and digestive functions of pest insects. The work brings us one step closer to the development of practical neuropeptide-like substances that will be effective in controlling pest insects in an environmentally friendly fashion.

Technical Abstract: Sulfakinins constitute a family of arthropod neuropeptides that typically contain the C-terminal heptapeptide Y(SO3H)GHMRFamide. They display structural and functional similarities to the vertebrate gastrin-cholecystokinin family of peptides. Sulfakinins are synthesized by a limited number of neurosecretory cells and exhibit several effects, including myotropic activities, inhibition of food intake, and stimulation of digestive enzyme release. In many cases, the sulfate group is a requirement for biological activity. The gastrin/CCK and sulfakinin signaling system is a good example of the coevolution of neuropeptides and their receptors.