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Published online on October 31, 2003, 10.1073/pnas.2231273100
PNAS | November 11, 2003 | vol. 100 | no. 23 | 13140-13145


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Chemistry
De novo designed cyclic-peptide heme complexes

Michael M. Rosenblatt *, Jiangyun Wang *, and Kenneth S. Suslick {dagger}

Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801

Edited by Harry B. Gray, California Institute of Technology, Pasadena, CA and approved September 2, 2003 (received for review March 4, 2002)

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.

This paper was submitted directly (Track II) to the PNAS office.

Abbreviation: NOE, nuclear Overhauser effect.

Data deposition: The atomic coordinates have been deposited in the Protein Data Bank, www.rcsb.org (PDB ID code 1PBZ).

* M.M.R. and J.W. contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: ksuslick{at}uiuc.edu.


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