Bombyxin exhibits an insulin-like response to modification in the N-terminal region of the A chain

Autor:	E E, Büllesbach
Rok vydání:	1999
Předmět:	Structure-Activity Relationship Magnetic Resonance Spectroscopy Sequence Homology Amino Acid Protein Conformation Swine Circular Dichroism Molecular Sequence Data Neuropeptides Animals Insulin Receptors Cell Surface Spectrophotometry Ultraviolet Amino Acid Sequence
Zdroj:	The journal of peptide research : official journal of the American Peptide Society. 54(1)
ISSN:	1397-002X
Popis:	Bombyxin is an insect neurohormone with an insulin-like structure. The N-terminal A chain helix, a region which is considered part of the active site in insulin, is almost identical between the two hormones. Bombyxin analogues with modifications at the N-terminus of the A-chain were synthesized and investigated for their ability to bind to bombyxin-specific receptors. While N-acetylation reduced the affinity to the bombyxin receptor to 18% the removal of glycine (A1) inactivated the hormone completely. Replacement of glycine (A1) by L-amino acids caused a significant loss in activity (11%) while its replacement by D-amino acid resulted in active bombyxin analogues (55%). Comparative CD spectroscopy indicated a change in structure for desGly(A1)bombyxin. Although the insect hormone does not have an insulin-like function it exhibits mammalian insulin-like structural sensitivity for A chain modifications.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::f3898d9e609cc1b535e174262eb61de2 https://pubmed.ncbi.nlm.nih.gov/10448965 Zobrazit plný text záznamu Plný text ve formátu PDF