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Chemical Synthesis and Characterization of an Equinatoxin II(1-85) Analogue.

ABSTRACT: The chemical synthesis of an 85 residue analogue of the pore-forming protein, Equinatoxin II (EqtII), was achieved. Peptide precursors with over 40 residues were assembled by solid phase synthesis. The EqtII(1-46) fragment was modified to the reactive C-terminal thioester and native chemical ligation was performed with the A47C mutated EqtII(47-85) peptide to form the EqtII(1-85) analogue. Circular dichroism spectroscopy indicated that the N-terminal domain of EqtII(1-46) and EqtII(1-85) maintains predominantly an ?-helical structure in solution and also in the presence of lipid micelles. This demonstrates the feasibility of assembling the full 179 residue protein EqtII via chemical means. Site-specific isotopic labels could be incorporated for structural studies in membranes by solid-state NMR spectroscopy.

SUBMITTER: Karas JA

PROVIDER: S-EPMC6153748 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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Chemical Synthesis and Characterization of an Equinatoxin II(1-85) Analogue.

Karas John A JA Sani Marc-Antoine MA Separovic Frances F

Molecules (Basel, Switzerland) 20170330 4

The chemical synthesis of an 85 residue analogue of the pore-forming protein, Equinatoxin II (EqtII), was achieved. Peptide precursors with over 40 residues were assembled by solid phase synthesis. The EqtII(1-46) fragment was modified to the reactive C-terminal thioester and native chemical ligation was performed with the A47C mutated EqtII(47-85) peptide to form the EqtII(1-85) analogue. Circular dichroism spectroscopy indicated that the N-terminal domain of EqtII(1-46) and EqtII(1-85) maintai ...[more]

PMID: 28358312

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