Structure-activity studies on adipokinetic hormones in Manduca sexta

✍ Scribed by Rolf Ziegler; Klaus Eckart; Ronald D. Jasensky; John H. Law

• Publisher: John Wiley and Sons
• Year: 1991
• Tongue: English
• Weight: 556 KB
• Volume: 18
• Category: Article
• ISSN: 0739-4462
• DOI: 10.1002/arch.940180405

✦ Synopsis

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'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 i n positions six and seven. Generally, the more amino acids are exchanged, the less the peptide will bind to the receptor. In M. sexta a P-bend appears not to be important for the binding of peptides. Peptides ten amino acids long appear to be more active than shorter ones.