Novel disintegrin‐like peptides derived from an amphibian skin cDNA sequence of Hypsiboas punctatus

2021 ◽  
Author(s):  
Diego A. T. Pires ◽  
Luisa M. R. A. Tacca ◽  
Joseph E. Aslan ◽  
André M. Murad ◽  
Claudia J. Nascimento ◽  
...  
Keyword(s):  
Cdna Sequence ◽  
Amphibian Skin

scholarly journals Discovery and Rational Design of a Novel Bowman-Birk Related Protease Inhibitor

Biomolecules ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 280 ◽  
Author(s):  
Yuxi Miao ◽  
Guanzhu Chen ◽  
Xinping Xi ◽  
Chengbang Ma ◽  
Lei Wang ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Inhibitory Activity ◽  
Rational Design ◽  
Cdna Sequence ◽  
Cell Penetrating Peptide ◽  
Skin Secretion ◽  
Amphibian Skin ◽  
Skin Secretions ◽  
Inhibitor Drug ◽  
Potent Inhibitory Activity

Anuran amphibian skin secretions are a rich source of peptides, many of which represent novel protease inhibitors and can potentially act as a source for protease inhibitor drug discovery. In this study, a novel bioactive Bowman-Birk type inhibitory hexadecapeptide of the Ranacyclin family from the defensive skin secretion of the Fukien gold-striped pond frog, Pelophlax plancyi fukienesis, was successfully isolated and identified, named PPF-BBI. The primary structure of the biosynthetic precursor was deduced from a cDNA sequence cloned from a skin-derived cDNA library, which contains a consensus motif representative of the Bowman-Birk type inhibitor. The peptide was chemically synthesized and displayed a potent inhibitory activity against trypsin (Ki of 0.17 µM), as well as an inhibitory activity against tryptase (Ki of 30.73 µM). A number of analogues of this peptide were produced by rational design. An analogue, which substituted the lysine (K) at the predicted P1 position with phenylalanine (F), exhibited a potent chymotrypsin inhibitory activity (Ki of 0.851 µM). Alternatively, a more potent protease inhibitory activity, as well as antimicrobial activity, was observed when P16 was replaced by lysine, forming K16-PPF-BBI. The addition of the cell-penetrating peptide Tat with a trypsin inhibitory loop resulted in a peptide with a selective inhibitory activity toward trypsin, as well as a strong antifungal activity. This peptide also inhibited the growth of two lung cancer cells, H460 and H157, demonstrating that the targeted modifications of this peptide could effectively and efficiently alter its bioactivity.

scholarly journals Molecular cloning of chick cardiac muscle tensin. Full-length cDNA sequence, expression, and characterization.

1994 ◽  
Vol 269 (35) ◽  
pp. 22310-22319
Author(s):  
S.H. Lo ◽  
Q. An ◽  
S. Bao ◽  
W.K. Wong ◽  
Y. Liu ◽  
...  
Keyword(s):  
Cardiac Muscle ◽  
Molecular Cloning ◽  
Cdna Sequence ◽  
Full Length ◽  
Full Length Cdna

scholarly journals Drosophila Cu-Zn superoxide dismutase cDNA sequence

1987 ◽  
Vol 15 (13) ◽  
pp. 5483-5483 ◽  
Author(s):  
Nina O.L. Seto ◽  
Shizu Hayashi ◽  
G.M. Tener
Keyword(s):  
Superoxide Dismutase ◽  
Cdna Sequence
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