期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 134, 期 12, 页码 5428-5431出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja2109079
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资金
- Otsuka Chmiecal Co. LTD.
- Osaka University
- Chicago University
- Sloan-Kettering Institute
- Columbia University
- Grants-in-Aid for Scientific Research [23245037] Funding Source: KAKEN
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.
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