Premium
Structure‐activity studies on adipokinetic hormones in Manduca sexta
Author(s) -
Ziegler Rolf,
Eckart Klaus,
Jasensky Ronald D.,
Law John H.
Publication year - 1991
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940180405
Subject(s) - manduca sexta , adipokinetic hormone , sphingidae , manduca , biology , biochemistry , amino acid , serine , peptide , glycogen phosphorylase , receptor , glycogen , enzyme , neuropeptide , insect , botany
Structure‐activity studies were performed for adipokinetic hormone (AKH) in Manduca sexta . Seven naturally occurring and four synthetic peptides of the red pigment concentrating hormone (RPCH)/AKH family were tested in larvae of M. sexta for activation of glycogen phosphorylase in fat body. pGlu at the N‐terminal was found to be important for activity of peptides; however, Manduca AcGly 1 AKH is partially active. The amino acids at all positions appear to be of importance for activity, with the possible exception of the two serine residues in positions six and seven. Generally, the more amino acids are exchanged, the less the peptide will bind to the receptor. In M. sexta a β‐bend appears not to be important for the binding of peptides. Peptides ten amino acids long appear to be more active than shorter ones.