Abstract：
:The present study purifies two T. serrulatus non-disulfide-bridged peptides (NDBPs), named venom peptides 7.2 (RLRSKG) and 8 (KIWRS) and details their synthesis and biological activity, comparing to the synthetic venom peptide 7.1 (RLRSKGKK), previously identified. The synthetic replicate peptides were subjected to a range of biological assays: hemolytic, antifungal, antiviral, electrophysiological, immunological and angiotensin-converting enzyme (ACE) inhibition activities. All venom peptides neither showed to be cytolytic nor demonstrated significant antifungal or antiviral activities. Interestingly, peptides were able to modulate macrophages' responses, increasing IL-6 production. The three venom peptides also demonstrated potential to inhibit ACE in the following order: 7.2>7.1>8. The ACE inhibition activity was unexpected, since peptides that display this function are usually proline-rich peptides. In attempt to understand the origin of such small peptides, we discovered that the isolated peptides 7.2 and 8 are fragments of the same molecule, named Pape peptide precursor. Furthermore, the study discusses that Pape fragments could be originated from a post-splitting mechanism resulting from metalloserrulases and other proteinases cleavage, which can be seen as a clever mechanism used by the scorpion to enlarge its repertoire of venom components. Scorpion venom remains as an interesting source of bioactive proteins and this study advances our knowledge about three NDBPs and their biological activities.
journal_name
Peptidesjournal_title
Peptidesauthors
Pucca MB,Cerni FA,Pinheiro-Junior EL,Zoccal KF,Bordon KCF,Amorim FG,Peigneur S,Vriens K,Thevissen K,Cammue BPA,Júnior RBM,Arruda E,Faccioli LH,Tytgat J,Arantes ECdoi
10.1016/j.peptides.2016.05.008subject
Has Abstractpub_date
2016-08-01 00:00:00pages
44-51eissn
0196-9781issn
1873-5169pii
S0196-9781(16)30091-2journal_volume
82pub_type
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