Abstract
| Language | English |
|---|---|
| Article number | 254 |
| Number of pages | 14 |
| Journal | Biomolecules |
| Volume | 9 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - 28 Jun 2019 |
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Keywords
- frog skin secretion; trypsin inhibitor; Kunitz-type inhibitors; kunitzins
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A Novel Kunitzin-Like Trypsin Inhibitor Isolated from Defensive Skin Secretion of Odorrana versabilis. / Dong, Yanjing; Shi, Daning ; Ying, Yuan; Xi, Xinping; Chen, Xiaoling; Wang, Lei; Zhou, Mei; Wu, Qinan ; Ma, Chengbang; Chen, Tianbao.
In: Biomolecules, Vol. 9, No. 7, 254, 28.06.2019.Research output: Contribution to journal › Article
TY - JOUR
T1 - A Novel Kunitzin-Like Trypsin Inhibitor Isolated from Defensive Skin Secretion of Odorrana versabilis
AU - Dong, Yanjing
AU - Shi, Daning
AU - Ying, Yuan
AU - Xi, Xinping
AU - Chen, Xiaoling
AU - Wang, Lei
AU - Zhou, Mei
AU - Wu, Qinan
AU - Ma, Chengbang
AU - Chen, Tianbao
PY - 2019/6/28
Y1 - 2019/6/28
N2 - Protease inhibitors that were identified from amphibian skin secretions with low molecular weights and potent inhibitory activity were thought to be potential candidates for novel peptide drugs. Here, a novel peptide with trypsin inhibitory activity was found in the skin secretion of the Chinese bamboo leaf odorous frog, Odorrana versabilis. Based on the sequence alignments of sequencing results, the novel peptide (ALKYPFRCKAAFC) was named as Kunitzin-OV. The synthetic replicate of Kunitzin-OV was subjected to a series of functional assays, and it exhibited a trypsin inhibitory activity with a Ki value of 3.042 µM, whereas, when Lys-9 at P1 position was substituted by Phe, trypsin inhibitory activity was undetected and the chymotrypsin inhibitory activity was optimized with a Ki value of 2.874 µM. However, its protease-binding loop was catabolized by trypsin during the trypsin cleavage test. In conclusion, Kunizin-OV is a novel peptide with trypsin inhibitory activity as a member of kunitzins, which is a non-typical Kunitz-like trypsin inhibitor with a highly conserved reactive site (K-A) and quite a short sequence.
AB - Protease inhibitors that were identified from amphibian skin secretions with low molecular weights and potent inhibitory activity were thought to be potential candidates for novel peptide drugs. Here, a novel peptide with trypsin inhibitory activity was found in the skin secretion of the Chinese bamboo leaf odorous frog, Odorrana versabilis. Based on the sequence alignments of sequencing results, the novel peptide (ALKYPFRCKAAFC) was named as Kunitzin-OV. The synthetic replicate of Kunitzin-OV was subjected to a series of functional assays, and it exhibited a trypsin inhibitory activity with a Ki value of 3.042 µM, whereas, when Lys-9 at P1 position was substituted by Phe, trypsin inhibitory activity was undetected and the chymotrypsin inhibitory activity was optimized with a Ki value of 2.874 µM. However, its protease-binding loop was catabolized by trypsin during the trypsin cleavage test. In conclusion, Kunizin-OV is a novel peptide with trypsin inhibitory activity as a member of kunitzins, which is a non-typical Kunitz-like trypsin inhibitor with a highly conserved reactive site (K-A) and quite a short sequence.
KW - frog skin secretion; trypsin inhibitor; Kunitz-type inhibitors; kunitzins
U2 - 10.3390/biom9070254
DO - 10.3390/biom9070254
M3 - Article
VL - 9
JO - Biomolecules
T2 - Biomolecules
JF - Biomolecules
SN - 2218-273X
IS - 7
M1 - 254
ER -