Strategies toward structural and functional 'optimization' of animal peptide toxins - Inserm - Institut national de la santé et de la recherche médicale Access content directly
Journal Articles International Journal of Medicine and Biomedical Research Year : 2012

Strategies toward structural and functional 'optimization' of animal peptide toxins

Abstract

Background: venoms of a variety of animal species (i.e. scorpions, snakes, spiders, sea anemones, marine cone snails, worms, and insects) are rich sources of bioactive compounds that possess obvious pharmacological, therapeutic and/or biotechnological values. A majority of these compounds are peptides that mainly target enzymes, membrane receptors or ion channels. Aim: In recent years, much efforts of researchers have been focused on characterizing and 'improving' the pharmacological profile of some venom toxins, mainly because of their structural/functional diversity and potential value as chemotherapeutic drugs in the treatment of specific human pathologies. Materials and methods: This study reviews the strategies towards optimization of animal peptide toxins. Results: These peptides are most often in a size range that allows their production in vitro by chemical synthesis or genetic engineering. Unfortunately, they rarely display the required characteristics in terms of selectivity, affinity, stability and targeting with regard to the desired application. During the last decade, a number of successful structural approaches or strategies have been developed to improve the intrinsic potential of venom peptides. Using different strategies (reviewed herein), a number of highly potent and selective toxinderived candidate drugs were designed and produced by chemical synthesis. Conclusion: Such strategies proved to be effective as several toxin-based drugs are already marketed while an increasing number of candidate chemotherapeutics are currently being developed in clinical phase.
Fichier principal
Vignette du fichier
Andreotti_2012_Strategies_ME.pdf (627.47 Ko) Télécharger le fichier
Origin : Publisher files allowed on an open archive
Loading...

Dates and versions

inserm-00843159 , version 1 (10-07-2013)

Identifiers

  • HAL Id : inserm-00843159 , version 1

Cite

Nicolas Andreotti, Helmi Ziadi, Stéphanie Mouhat, Michel de Waard, Jean-Marc Sabatier. Strategies toward structural and functional 'optimization' of animal peptide toxins. International Journal of Medicine and Biomedical Research, 2012, 1 (2), pp.91-96. ⟨inserm-00843159⟩
94 View
275 Download

Share

Gmail Facebook X LinkedIn More