Control of peptide structure and recognition by Fe(III)-induced helix destabilization.
Helical peptide segments that change their conformation due to external stimuli have often been employed in peptide-based molecular devices and materials. Using helices containing a pair of the iminodiacetic acid derivatives of lysine (Ida), we show that metal-induced helix destabilization is a promising approach to functional switching, especially for helices that are intrinsically stable. By i and i + 2 positioning of the Ida residues in a 17-residue model peptide, a significant decrease in the helical content was observed by the addition of Fe(III), whereas Fe(II) had no influence on the stability of the helix. The possibility of redox control of the helical structure was exemplified by the reduction of Fe(III) to Fe(II) using Na(2)S(2)O(4) followed by the subsequent reoxidation. Mutual recognition of the transcription factor Jun-derived leucine-zipper peptide segment with the Fos leucine-zipper segment containing Ida residues was also modulated in the presence of Fe(III).
Futaki
Shiroh
S
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan. futaki@sci.kyoto-u.ac.jp
Kiwada
Tatsuto
T
Sugiura
Yukio
Y
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D005290:Ferric Compounds / Q000737:chemistry*; D007098:Imino Acids / Q000737:chemistry*; D008969:Molecular Sequence Data; D016759:Oncogene Protein p65(gag-jun) / Q000737:chemistry; D016761:Oncogene Proteins v-fos / Q000737:chemistry; D010084:Oxidation-Reduction; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013056:Spectrophotometry, Ultraviolet
D005290:Ferric Compounds; D007098:Imino Acids; D016759:Oncogene Protein p65(gag-jun); D016761:Oncogene Proteins v-fos; D010455:Peptides; C008109:iminodiacetic acid