Correct disulfide pairing is required for the biological activity of crustacean androgenic gland hormone (AGH): synthetic studies of AGH.
Biochemistry
; 49(8): 1798-807, 2010 Mar 02.
Article
in En
| MEDLINE
| ID: mdl-20092253
ABSTRACT
Androgenic gland hormone (AGH) of the woodlouse, Armadillidium vulgare, is a heterodimeric glycopeptide. In this study, we synthesized AGH with a homogeneous N-linked glycan using the expressed protein ligation method. Unexpectedly, disulfide bridge arrangement of a semisynthetic peptide differed from that of a recombinant peptide prepared in a baculovirus expression system, and the semisynthetic peptide showed no biological activity in vivo. To confirm that the loss of biological activity resulted from disulfide bond isomerization, AGH with a GlcNAc moiety was chemically synthesized by the selective disulfide formation. This synthetic AGH showed biological activity in vivo. These results indicate that the native conformation of AGH is not the most thermodynamically stable form, and correct disulfide linkages are important for conferring AGH activity.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Gonadal Hormones
Limits:
Animals
Language:
En
Journal:
Biochemistry
Year:
2010
Document type:
Article
Affiliation country:
Japan