Protease inhibitors have an important role controlling a variety of biological processes. Here, we employed a peptidomic approach including molecular cloning, tandem mass spectrometry and enzymatic assays to reveal 7 Kazal-type proteinase inhibitors (CCKPs) (18 variants) in the skin secretion of the unexplored frog, Cruziohyla calcarifer. All 18 proteins shared the Kazal pattern (CX(6-7)-CX(6-7)-Y-X(2-3)-CX(2)-C) and 3 disulphide bridges. Based on structural comparative analysis, we deemed trypsin and chymotrypsin inhibitory activity in CCKP-1, 4 and CCKP 2, 5, 7, respectively. These protease inhibitors presumably play a role to control the balance between other functional peptides produced in the amphibian skin secretions.
|Number of pages||13|
|Journal||EuPA Open Proteomics|
|Early online date||27 Feb 2017|
|Publication status||Published - Jun 2017|
- Kazal-type proteinase inhibitors; frog skin secretion; peptidomic; molecular cloning; tandem mass spectrometry; Cruziohyla calcarifer