Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 16, Issue 22, Pages 6651-6659Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.200903092
Keywords
biocompatibility; rhodium; helical structures; metallopeptides; secondary structures
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Funding
- J. Evans Attwell-Welch Post-Doctoral Fellowship
- Robert A. Welch Foundation [C-1680]
- Rice University
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The use of carboxylate side chains to induce peptide helicity upon binding to dirhodium centers is examined through experimental and computational approaches. Dirhodium binding efficiently stabilizes a helicity or induces a helicity in otherwise unstructured peptides for peptides that contain carboxylate side chains with i, i+4 spacing. Helix induction is furthermore possible for sequences with i, i+3 carboxylate spacing, though in this case the length of the side chains is crucial: ligating to longer glutamate side chains is strongly helix inducing, whereas ligating the shorter aspartate side chains destabilizes the helical structure. Further studies demonstrate that a dirhodium metallopeptide complex persists for hours in cellular media and exhibits low toxicity toward mammalian cells, enabling exploitation of these metallopeptides for biological applications.
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