Scorpion venom peptides with no disulfide bridges: a review

Peptides. 2014 Jan;51:35-45. doi: 10.1016/j.peptides.2013.10.021. Epub 2013 Oct 31.


Scorpion venoms are rich sources of biologically active peptides that are classified into disulfide-bridged peptides (DBPs) and non-disulfide-bridged peptides (NDBPs). DBPs are the main scorpion venom components responsible for the neurotoxic effects observed during scorpion envenomation as they usually target membrane bound ion channels of excitable and non-excitable cells. Several hundred DBPs have been identified and functionally characterized in the past two decades. The NDBPs represent a novel group of molecules that have gained great interest only recently due to their high diversity both in their primary structures and bioactivities. This review provides an overview of scorpion NDBPs focusing on their therapeutic applications, modes of discovery, mechanisms of NDBPs genetic diversity and structural properties. It also provides a simple classification for NDBPs that could be adopted and applied to other NDBPs identified in future studies.

Keywords: Anticancer; Antimicrobial; Classification; NDBPs; Non-disulfide-bridged peptides; Scorpion; Structural properties; Venom.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / pharmacology
  • Antimalarials / chemistry
  • Antimalarials / pharmacology
  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / pharmacology
  • Arthropod Proteins / chemistry*
  • Arthropod Proteins / pharmacology
  • Cystine / chemistry*
  • Humans
  • Molecular Sequence Data
  • Scorpion Venoms / chemistry*
  • Scorpion Venoms / pharmacology
  • Scorpions / metabolism*
  • Vasodilator Agents / chemistry
  • Vasodilator Agents / pharmacology


  • Anti-Infective Agents
  • Antimalarials
  • Antineoplastic Agents
  • Arthropod Proteins
  • Scorpion Venoms
  • Vasodilator Agents
  • Cystine