A 1H-NMR study of the solution conformation of Icaria chemotactic peptide and its [Lys7] analog: effects on the physiological activity of a substitution of proline to lysine at position 7.
Solution conformations of Icaria chemotactic peptide isolated from the Ropalidian wasp venom and its [Lys7] analog have been analyzed by the use of two-dimensional proton nuclear resonance spectroscopy. It has been shown that Icaria chemotactic peptide takes alpha helical conformation in the C-terminal 8-13 segment with the N-terminal 1-7 segment disordered. By contrast, the [Lys7] analog takes alpha helical conformation over a wider range from residues 3 to 13. The present results indicate that the substitution of proline to lysine at position 7 results in a drastic change in solution conformation, providing the Icaria chemotactic peptide with new physiological functions.
Shimada
I
I
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Kato
K
K
Saito
K
K
Kitada
C
C
Fujino
M
M
Nakajima
T
T
Arata
Y
Y
D000595:Amino Acid Sequence; D002630:Chemotactic Factors / Q000502:physiology; D008239:Lysine / Q000235:genetics; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009154:Mutation; D010449:Peptide Mapping; D011392:Proline / Q000235:genetics; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D002630:Chemotactic Factors; C063920:Icaria chemotactic peptide, Lys(7)-; C063906:Icaria chemotactic peptide; D011392:Proline; D008239:Lysine