AI Article Synopsis
- A new protein called PPTI was discovered in the venom of the Persian false horned viper and is part of the kunitz-type protein family.
- Mass spectrometry revealed that PPTI is a 68 amino acid protein with unique traits, including a pyroglutamyl modification at its N-terminus.
- The study suggests that PPTI can inhibit trypsin and may also block potassium channels, indicating it has dual functionality.
Article Abstract
A new member of kunitz-type protein family, PPTI (PseudocerastesPersicusTrypsin Inhibitor), was isolated from the venom of Persian false horned viper Pseudocerastes persicus and characterized. Mass spectrometry and amino acid sequencing revealed that PPTI is a 68 amino acid protein with molecular weight of about 7.6 kDa. The first amino acid residue of PPTI is N-terminally blocked via a post translational modification to pyroglutamyl. Sequence comparison against UniProtKB shows a high sequence similarity of PPTI with kunitz-type proteins, especially serine protease inhibitors and dendrotoxins (DTXs). The number of cysteines and disulfide bonding pattern of PPTI are the same as kunitz-type proteins. Based on sequence derive information, anti-protease activity of PPTI against trypsin was experimentally examined. The constructed homology models of PPTI confirmed the ability of PPTI to fold similarly to kunitz domain. The presence of characteristic basic-hydrophobic functional dyad of DTXs in PPTI supports its inhibitory potential against potassium channels. In summary, this study hypothesized the dual functionality of PPTI according to its inhibitory effect on trypsin and its potential ability in blocking potassium channel.
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| http://dx.doi.org/10.1016/j.abb.2018.11.017 | DOI Listing |
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