Proteomic analysis of the venom of Heterometrus longimanus (Asian black scorpion).
Venoms have evolved over millions of years into potent cocktails of bioactive peptides and proteins. These compounds can be of great value to the pharmaceutical industry for numerous clinical applications. In this study, a novel proteomic - bioinformatic approach was utilised, where chromatography followed by gel electrophoresis was utilised to separate the venom peptides/proteins of Heterometrus longimanus (Asian black scorpion). Purified peptides were analysed by tandem mass spectrometry, de novo sequenced and then homology matched against known peptides in the Swiss-Prot protein database. Numerous potentially biologically active peptide matches were discovered, and a simple scoring system applied to putatively assign functions to the peptides. As a validation of this approach, the functional composition of the experimentally derived proteome is similar to that of other scorpions, and contains a potent mix of toxins, antimicrobials and ionic channel inhibitors.
Bringans
Scott
S
Proteomics International, Perth, Western Australia, Australia. scott@proteomics.com.au
Eriksen
Soren
S
Kendrick
Tulene
T
Gopalakrishnakone
P
P
Livk
Andreja
A
Lock
Robert
R
Lipscombe
Richard
R
D000818:Animals; D010455:Peptides / Q000032:analysis; D040901:Proteomics; D012604:Scorpion Venoms / Q000737:chemistry*; D012605:Scorpions; D020539:Sequence Analysis, Protein; D053719:Tandem Mass Spectrometry / Q000379:methods*
D010455:Peptides; D012604:Scorpion Venoms