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Scorpion venom contains various bioactive peptides. Among them, peptides having two different structural domains constitute a toxin family known as β‐KTx or scorpine‐like peptides. These peptides consist of an α‐helical structure in the N‐terminal region and a cysteine‐stabilized structure in the C‐terminal region. This unique structure of β‐KTx peptides contributes to their diverse biological functions,...
La1 is a 73‐residue cysteine‐rich peptide isolated from the scorpion Liocheles australasiae venom. Although La1 is the most abundant peptide in the venom, its biological function remains unknown. Here, we describe a method for efficient chemical synthesis of La1 using the native chemical ligation (NCL) strategy, in which three peptide components of less than 40 residues were sequentially ligated....
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