Abstract
The circular dichroism (CD) spectrum of ω-conotoxin GVIA is quite different from those of ω-conotoxin MVIIA and MVIIC, despite their distinct similarity in three dimensional structures. In order to characterize the unique CD spectrum of ω-conotoxin GVIA, we focused our attention on the aromatic chromophore and analyzed the CD spectra of three synthetic analogs, in which Tyr13, Tyr22, and Tyr27were individually replaced by alanine. Replacement of Tyr27caused a significant change in both the near- and far-ultraviolet CD spectrum of ω-conotoxin GVIA and resulted in the ω-conotoxin MVIIA/MVIIC-like pattern, suggesting that Tyr27has a dominant contribution to the unique CD profile of ω-conotoxin GVIA.
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