期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 138, 期 43, 页码 14214-14217出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.6b09454
关键词
-
资金
- NIH [GM107036]
- NSF [CBET-0952875]
Lasso peptides exist naturally in a threaded state as [1]rotaxanes, and we reasoned that lasso peptides cleaved in their loop region could serve as building:blocks for catenaries. Mutagenesis of the lasso peptide microcin J25 (MccJ25) with two cysteine residues followed by cleavage of the peptide with trypsin. led to a [2]rotaxane structure that self-assembled into a [3]catenane and [4]catenanes at room temperature in aqueous solution. The [3]catenane represents the smallest ring size of a catenane composed solely of polypeptide segments. The NMR structure of the [3]catenane was determined, suggesting that burial of hydrophobic residues may be a driving force for assembly of the catenane structure.
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