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• W2079498547 abstract "Venoms of the predatory cone snails Conus textile, Conus striatus, and Conus magus were subjected to comprehensive analysis of peptide content. With the fish-eating cone snails C. magus and C. striatus, the most abundant venom peptides were of > 30–50 residues, whereas the predominant peptides in the venom of the mollusceating snail, C. textile, were of 20–35 residues. Amino acid sequencing revealed an identical but unusual amino acid in a conserved position in four novel ω-type peptides from the C. textile venom. Two conserved amino acid sequences were obtained from the venoms of both C. magus and C. striatus. The amino acid compositions of the isolated C. textile peptides and the expected processing products of the propeptides (42) were compared. Despite the recovery in abundance of the carboxyl-terminal ω-type peptides, none of the isolated peptides had compositions expected from the propeptide amino-terminal fragments. We conclude that there are likely mechanisms for excluding the amino-terminal propeptide fragments from this venom, resulting in a venom with greater potency. Amounts of the different ω-type peptides in the venom vary widely, suggesting a distinct mechanism that results in the selective synthesis of different bioactive carboxyl-terminal propeptide fragments at elevated levels." @default.
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• W2079498547 date "1995-01-01" @default.
• W2079498547 modified "2023-10-14" @default.
• W2079498547 title "Structural and biosynthetic properties of peptides in cone snail venoms" @default.
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• W2079498547 doi "https://doi.org/10.1016/0196-9781(95)00086-y" @default.
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