ArticleThe Journal of organic chemistry2011
Giant macrolactams based on β-sheet peptides.
Article in The Journal of organic chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids.Nature chemistry · 2018Article
- Diversification of β-Augmentation Interactions between CDI Toxin/Immunity Proteins.Journal of molecular biology · 2015Article
- Peptide amyloid surface display.Biochemistry · 2015Article
- Convergent diversity-oriented side-chain macrocyclization scan for unprotected polypeptides.Organic & biomolecular chemistry · 2014Article
- The supramolecular chemistry of β-sheets.Journal of the American Chemical Society · 2013Review
- Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity.Nature chemistry · 2012Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
This paper reports the use of natural amino acids, the tripeptide β-strand mimic Hao, and the β-turn mimic δ-linked ornithine to generate water-soluble 54-, 78-, and 102-membered-ring macrolactams. These giant macrocycles were efficiently prepared by synthesis of the corresponding protected linear peptides, followed by solution-phase cyclization and deprotection. The protected linear peptide precursors were synthesized on 2-chlorotrityl chloride resin by conventional Fmoc-based solid-phase peptide synthesis. Macrocyclization was typically performed using HCTU and N,N-diisopropylethylamine in DMF at ca. 0.5 mM concentration. The macrocycles were isolated in 13-45% overall yield after HPLC purification and lyophilization. 1D, 2D TOCSY, and 2D ROESY (1)H NMR studies of the 54- and 78-membered-ring macrolactams establish that these compounds fold to form β-sheet structures in aqueous solutions.
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Registered trials
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