Circular dichroism spectra of calcium channel antagonist omega-conotoxins.
The circular dichroism (CD) spectrum of omega-conotoxin GVIA is quite different from those of omega-conotoxin MVIIA and MVIIC, despite their distinct similarity in three dimensional structures. In order to characterize the unique CD spectrum of omega-conotoxin GVIA, we focused our attention on the aromatic chromophore and analyzed the CD spectra of three synthetic analogs, in which Tyr13, Tyr22, and Tyr27 were individually replaced by alanine. Replacement of Tyr27 caused a significant change in both the near- and far-ultraviolet CD spectrum of omega-conotoxin GVIA and resulted in the omega-conotoxin MVIIA/MVIIC-like pattern, suggesting that Tyr27 has a dominant contribution to the unique CD profile of omega-conotoxin GVIA.
Kim
J I
JI
Mitsubishi Kasei Institute of Life Sciences, Machida-shi, Tokyo, Japan.
Ohtake
A
A
Sato
K
K
D000409:Alanine; D000595:Amino Acid Sequence; D002121:Calcium Channel Blockers / Q000737:chemistry*; D002942:Circular Dichroism; D004220:Disulfides; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D014443:Tyrosine; D020866:omega-Conotoxin GVIA; D020960:omega-Conotoxins
D002121:Calcium Channel Blockers; D004220:Disulfides; D010455:Peptides; D020960:omega-Conotoxins; C075851:omega-conotoxin-MVIIC; D014443:Tyrosine; C078452:ziconotide; D020866:omega-Conotoxin GVIA; D000409:Alanine