Serrulin: a glycine-rich bioactive peptide from the hemolymph of the yellow Tityus serrulatus scorpion

Publication type
Access rights
Open Access
Appears in Collections:
Antimicrobial peptides (AMPs) are small molecules, which have a potential use as antibiotic or pharmacological tools. In chelicerate organisms, such as scorpions, these molecules constitute an alternative defense system against microorganisms. The aim of this work was to identify AMPs in the hemolymph of the Tityus serrulatus scorpion. Fractions of plasma and hemocytes were subjected to high-performance liquid chromatography (HPLC) and then analyzed to determine their activity in inhibiting microbial growth. One of the fractions from the hemocytes presents antimicrobial activity against microorganisms, such as Gram-negative and Gram-positive bacteria, fungi, and yeast. These fractions were analyzed by mass spectrometry, and a fragment of 3564 Da. was identified. The peptide was called serrulin, because it is derived from the species T. serrulatus. A comparison of the amino acid sequence of serrulin with databases shows that it has a similarity to the glycine-rich peptides described in Cupienius salai and Acanthoscurria gomesiana (spiders). Furthermore, serrulin has no hemolytic activity against human erythrocytes. While the presence of AMPs in T. serrulatus venom has been described in other works, this is the first work to characterize the presence of these molecules in the hemolymph (hemocytes) of this species and show its potential use as an alternative to conventional antibiotics against different species of microorganisms.
Oliveira TJ, Oliveira UC, Silva Junior PI. Serrulin: a glycine-rich bioactive peptide from the hemolymph of the yellow Tityus serrulatus scorpion. Toxins. 2019 Sep;11(9):517. doi:10.3390/toxins11090517.
Link to cite this reference
Journal title
Issue Date

Files in This Item:

Size: 1.43 MB
Format: Adobe PDF
Show full item record

The access to the publications deposited in this repository respects the licenses from journals and publishers.