Minimum structure of diapause hormone required for biological activity.
Diapause hormone is a 24-amino acid peptide amide, and its C-terminal penta-peptide amide structure of FGPRL-NH2 is believed to be essential for biological activity. The penta-peptide amide, the shorter peptide amides, and their derivatives and analogs were prepared to determine the minimal structure for biological activity. The C-terminal amide group of penta-peptide amide was not replaced with the other functional groups, but Gly, the 4th amino acid from the C terminal, could be substituted with an other amino acid while maintaining the biological activity. The shorter peptide amide, PRL-NH2, possessed low but significant activity, indicating the minimum structure of diapause hormone. By modifying its N-terminal, the aromatic ring of Phe is shown to enhance the activity of PRL-NH2.
Imai
K
K
School of Bio-resources, Mie University, Japan. imai@bio.mie-u.ac.jp
Nomura
T
T
Katsuzaki
H
H
Komiya
T
T
Yamashita
O
O
D000818:Animals; D012831:Bombyx / Q000187:drug effects / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D009479:Neuropeptides / Q000737:chemistry* / Q000494:pharmacology; D009842:Oligopeptides / Q000138:chemical synthesis / Q000494:pharmacology; D013329:Structure-Activity Relationship
D009479:Neuropeptides; D009842:Oligopeptides; C116219:phenylalanyl-glycyl-prolyl-arginyl-leucinamide; C075027:diapause hormone