De novo designed cyclic-peptide heme complexes
AUTOR(ES)
Rosenblatt, Michael M.
FONTE
National Academy of Sciences
RESUMO
The structural characterization of de novo designed metalloproteins together with determination of chemical reactivity can provide a detailed understanding of the relationship between protein structure and functional properties. Toward this goal, we have prepared a series of cyclic peptides that bind to water-soluble metalloporphyrins (FeIII and CoIII). Neutral and positively charged histidine-containing peptides bind with a high affinity, whereas anionic peptides bind only weakly to the negatively charged metalloporphyrin. Additionally, it was found that the peptide becomes helical only in the presence of the metalloporphyrin. CD experiments confirm that the metalloporphyrin binds specific cyclic peptides with high affinity and with isodichroic behavior. Thermal unfolding experiments show that the complex has ”native-like” properties. Finally, NMR spectroscopy produced well dispersed spectra and experimental restraints that provide a high-resolution solution structure of the complexed peptide.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=263730Documentos Relacionados
- De novo designed peptide-based amyloid fibrils
- Cyclic amphipathic peptide-DNA complexes mediate high-efficiency transfection of adherent mammalian cells.
- De novo amyloid proteins from designed combinatorial libraries
- A designed beta-hairpin peptide in crystals.
- Programming peptidomimetic syntheses by translating genetic codes designed de novo