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Helix Induction by Dirhodium: Access to Biocompatible Metallopeptides with Defined Secondary Structure
Author(s) -
Zaykov Alexander N.,
Popp Brian V.,
Ball Zachary T.
Publication year - 2010
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200903092
Subject(s) - carboxylate , side chain , helix (gastropod) , helicity , peptide , chemistry , stereochemistry , biocompatible material , alpha helix , circular dichroism , biochemistry , physics , biology , organic chemistry , polymer , medicine , ecology , particle physics , snail , biomedical engineering
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 α helicity or induces α 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.