Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 134, Issue 12, Pages 5428-5431Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja2109079
Keywords
-
Categories
Funding
- Otsuka Chmiecal Co. LTD.
- Osaka University
- Chicago University
- Sloan-Kettering Institute
- Columbia University
- Grants-in-Aid for Scientific Research [23245037] Funding Source: KAKEN
Ask authors/readers for more resources
Chemical synthesis of homogeneous human glycoproteins exhibiting bioactivity in vivo has been a challenging task. In an effort to overcome this long-standing problem, we selected interferon-beta and examined its synthesis. The 166 residue polypeptide chain of interferon-beta was prepared by covalent condensation of two synthetic peptide segments and a glycosylated synthetic peptide bearing a complex-type glycan of biological origin. The peptides were covalently condensed by native chemical ligation. Selective desulfurization followed by deprotection of the two Cys(Acm) residues gave the target full-length polyp eptide chain of interferon-beta bearing either a complex-type sialyl biantennary oligosaccharide or its asialo form. Subsequent folding with concomitant formation of the native disulfide bond afforded correctly folded homogeneous glycosyl-interferon-beta. The chemically synthesized sialyl interferon-beta exhibited potent antitumor activity in vivo.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available