A Novel Trypsin Inhibitor-Like Cysteine-Rich Peptide from the Frog <i>Lepidobatrachus laevis</i> Containing Proteinase Inhibiting Activity

doi:10.1007/s13659-015-0069-z

Natural Products and Bioprospecting

2015, Vol. 5

Issue (4) : 209-214 DOI: 10.1007/s13659-015-0069-z

Original article

A Novel Trypsin Inhibitor-Like Cysteine-Rich Peptide from the Frog Lepidobatrachus laevis Containing Proteinase Inhibiting Activity

Yu-Wei Wang¹, Ji-Min Tan¹, Can-Wei Du¹, Ning Luan¹, Xiu-Wen Yan¹, Ren Lai^1,2, Qiu-Min Lu²

1. Life Sciences College of Nanjing Agricultural University, Nanjing 210095, Jiangsu, China;
2. Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences&Yunnan Province, Kunming Institute of Zoology, Kunming 650223, Yunnan, China

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Abstract Various bio-active substances in amphibian skins play important roles in survival of the amphibians. Many protease inhibitor peptides have been identified from amphibian skins, which are supposed to negatively modulate the activity of proteases to avoid premature degradation or release of skin peptides, or to inhibit extracellular proteases produced by invading bacteria. However, there is no information on the proteinase inhibitors from the frog Lepidobatrachus laevis which is unique in South America. In this work, a cDNA encoding a novel trypsin inhibitor-like(TIL) cysteine-rich peptide was identified from the skin cDNA library of L. laevis. The 240-bp coding region encodes an 80-amino acid residue precursor protein containing 10 half-cysteines. By sequence comparison and signal peptide prediction, the precursor was predicted to release a 55-amino acid mature peptide with amino acid sequence, IRCPKDKIYKFCGSPCPPSCKDLTPNCIAVCKKGCFCRDGTVDNNHGKCVKKENC. The mature peptide was named LL-TIL. LL-TIL shares significant domain similarity with the peptides from the TIL supper family. Antimicrobial and trypsin-inhibitory abilities of recombinant LL-TIL were tested. Recombinant LL-TIL showed no antimicrobial activity, while it had trypsin-inhibiting activity with a Ki of 16.5178 μM. These results suggested there was TIL peptide with proteinase-inhibiting activity in the skin of frog L. laevis. To the best of our knowledge, this is the first report of TIL peptide from frog skin.

Keywords Trypsin inhibitor Cysteine-rich peptide Amphibian Skin

Fund:This work was supported by grants from the China National Natural Science Foundation of Young Scientists(No. 31201717), Special Foundation for Young Scientists of Jiangsu Province(No. BK2012365), Jiangsu Province Science and Technology Support Project(No. BE2012748).

Issue Date: 11 February 2018

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Yu-Wei Wang,Ji-Min Tan,Can-Wei Du, et al. A Novel Trypsin Inhibitor-Like Cysteine-Rich Peptide from the Frog Lepidobatrachus laevis Containing Proteinase Inhibiting Activity[J]. Natural Products and Bioprospecting, 2015, 5(4): 209-214.

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http://npb.kib.ac.cn/EN/10.1007/s13659-015-0069-z OR http://npb.kib.ac.cn/EN/Y2015/V5/I4/209

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