Protease-mediated ligation of abiotic oligomers.
We demonstrate that proteases can catalyze the ligation of peptidomimetic oligomers. The enzyme clostripain was used to facilitate the native ligation of N-substituted glycine oligomers, or peptoids. In addition to mediating the efficient condensation of two peptoid fragments, iterative ligation events were also performed, giving rise to concatenation products with molecular weights up to 20 kDa. Efficient ligation of peptoid foldamers may enable the chemical synthesis of biomimetic macromolecules capable of forming complex tertiary structures.
Yoo
Barney
B
Department of Chemistry, New York University, 100 Washington Square East, New York, New York 10003-6688, USA.
Kirshenbaum
Kent
K
D003546:Cysteine Endopeptidases / Q000378:metabolism*; D034444:Peptoids / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation
D034444:Peptoids; D003546:Cysteine Endopeptidases; C019913:clostripain