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Peptide-based Identification of Functional Motifs and their Binding Partners
Published on: June 30, 2013
Two N-terminally truncated forms of C-type natriuretic peptide from habu snake venom
G H Michel1, N Murayama, T Sada
1School of Pharmaceutical Sciences, Showa University, Hatanodai, Shinagawa-ku, 142-8555, Tokyo, Japan.
Insights
Researchers discovered two shorter forms of C-type natriuretic peptide (CNP) in habu snake venom. One form, Tf-CNP(6-22), is the shortest natural CNP and shows potent vasorelaxant and diuretic effects.
Area of Science:
- Biochemistry
- Pharmacology
- Herpetology
Background:
- C-type natriuretic peptide (CNP) plays crucial roles in cardiovascular and renal functions.
- Snake venom is a rich source of biologically active peptides with therapeutic potential.
Purpose of the Study:
- To isolate and characterize novel CNP variants from Trimeresurus flavoviridis (habu snake) venom.
- To investigate the biological activities of these novel CNP forms.
Main Methods:
- Isolation of peptides from habu snake venom.
- Structural determination using Electrospray Ionization Mass Spectrometry (ESI-MS) and amino acid sequencing.
- Assessment of vasorelaxant activity in rat aortic strips.
- Evaluation of diuretic potency in anesthetized rats.
Main Results:
- Two N-terminally truncated CNP forms were identified: Tf-CNP(6-22) and Tf-CNP(3-22).
- Tf-CNP(6-22), a 17-amino acid peptide with a disulfide bridge, exhibited significant vasorelaxant and diuretic activities.
- Tf-CNP(6-22) is the shortest naturally occurring CNP identified to date and demonstrated potency comparable to the full-length CNP (Tf-CNP(1-22)).
Conclusions:
- Novel, truncated CNP variants exist in habu snake venom.
- The minimal 17-residue ring structure of CNP is sufficient for potent biological activity.
- These findings expand our understanding of CNP diversity and function, with potential implications for drug discovery.
Abstract:
Two N-terminally truncated forms of the C-type natriuretic peptide (CNP) were isolated from the venom of habu snake, Trimeresurus flavoviridis, and their structures were determined by EMI-MS spectrometry and amino acid sequencing. Tf-CNP(6-22), the shorter peptide retaining the 17-membered ring structure formed by an intra-molecular disulfide bridge, has a vasorelaxant activity in rat aortic strips and a diuretic potency in anesthetized rats. Tf-CNP(3-22), the other 20 amino acid residues peptide, also comprised the 17- membered ring with a short N-terminal extension of 3 amino acid residues. Tf-CNP(6-22), the ring, is the shortest naturally occurring CNP peptide identified so far, and as potent as Tf-CNP(1-22), the supposedly intact CNP of 22 amino acid residues.
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