Correct Disulfide Pairing Is Required for the Biological Activity of Crustacean Androgenic Gland Hormone (AGH): Synthetic Studies of AGH

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 fr...

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Published in:Biochemistry (Easton) 2010-03, Vol.49 (8), p.1798-1807
Main Authors: Katayama, Hidekazu, Hojo, Hironobu, Ohira, Tsuyoshi, Ishii, Akira, Nozaki, Takamichi, Goto, Kiyomi, Nakahara, Yuko, Takahashi, Tetsuo, Hasegawa, Yuriko, Nagasawa, Hiromichi, Nakahara, Yoshiaki
Format: Article
Language:English
Subjects:
Animals
Armadillidium vulgare
Baculovirus
Crustacea
Electrophoresis, Polyacrylamide Gel
Gonadal Hormones - chemical synthesis
Gonadal Hormones - chemistry
Gonadal Hormones - metabolism
Magnetic Resonance Spectroscopy
Models, Biological
Molecular Structure
Thermodynamics
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Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi902100f