Semisynthesis of Peptoid-Protein Hybrids by Chemical Ligation at Serine

被引:32
|
作者
Levine, Paul M. [1 ]
Craven, Timothy W. [2 ]
Bonneau, Richard [2 ,3 ]
Kirshenbaum, Kent [1 ]
机构
[1] NYU, Dept Chem, New York, NY 10003 USA
[2] NYU, Ctr Genom & Syst Biol, New York, NY 10003 USA
[3] NYU, Courant Inst Math Sci, Dept Comp Sci, New York, NY 10012 USA
基金
美国国家科学基金会;
关键词
PEPTIDE; THREONINE; SCAFFOLD; HORMONE; SITE;
D O I
10.1021/ol4033978
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
Chemical ligation protocols were explored for generating semisynthetic peptoid-protein hybrid architectures containing a native serine residue at the ligation site. Peptoid oligomers bearing C-terminal salicylaldehyde esters were synthesized and ligated to the N-terminus of the RNase S protein or the therapeutic hormone PTH(1-34) polypeptide. This technique will expand the repertoire of strategies to enable design of hybrid macromolecules with novel structures and functions not accessible to fully biosynthesized proteins.
引用
收藏
页码:512 / 515
页数:4
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