Chemical Synthesis and Characterization of an Equinatoxin II(1–85) Analogue
AbstractThe 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 α-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. View Full-Text
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Karas, J.A.; Sani, M.-A.; Separovic, F. Chemical Synthesis and Characterization of an Equinatoxin II(1–85) Analogue. Molecules 2017, 22, 559.
Karas JA, Sani M-A, Separovic F. Chemical Synthesis and Characterization of an Equinatoxin II(1–85) Analogue. Molecules. 2017; 22(4):559.Chicago/Turabian Style
Karas, John A.; Sani, Marc-Antoine; Separovic, Frances. 2017. "Chemical Synthesis and Characterization of an Equinatoxin II(1–85) Analogue." Molecules 22, no. 4: 559.
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