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    Macrocyclic β-Sheet Peptides That Mimic Protein Quaternary Structure through Intermolecular β-Sheet Interactions
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    Contribution from the Department of Chemistry, University of CaliforniaIrvine, Irvine, California 92697-2025, and Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78229
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2007, 129, 17, 5558–5569
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    https://doi.org/10.1021/ja068511u
    Published April 10, 2007
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    Abstract

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    This paper reports the design, synthesis, and characterization of a family of cyclic peptides that mimic protein quaternary structure through β-sheet interactions. These peptides are 54-membered-ring macrocycles comprising an extended heptapeptide β-strand, two Hao β-strand mimics [JACS2000, 122, 7654] joined by one additional α-amino acid, and two δ-linked ornithine β-turn mimics [JACS2003, 125, 876]. Peptide 3a, as the representative of these cyclic peptides, contains a heptapeptide sequence (TSFTYTS) adapted from the dimerization interface of protein NuG2 [PDB ID:  1mio]. 1H NMR studies of aqueous solutions of peptide 3a show a partially folded monomer in slow exchange with a strongly folded oligomer. NOE studies clearly show that the peptide self-associates through edge-to-edge β-sheet dimerization. Pulsed-field gradient (PFG) NMR diffusion coefficient measurements and analytical ultracentrifugation (AUC) studies establish that the oligomer is a tetramer. Collectively, these experiments suggest a model in which cyclic peptide 3a oligomerizes to form a dimer of β-sheet dimers. In this tetrameric β-sheet sandwich, the macrocyclic peptide 3a is folded to form a β-sheet, the β-sheet is dimerized through edge-to-edge interactions, and this dimer is further dimerized through hydrophobic face-to-face interactions involving the Phe and Tyr groups. Further studies of peptides 3b−3n, which are homologues of peptide 3a with 1−6 variations in the heptapeptide sequence, elucidate the importance of the heptapeptide sequence in the folding and oligomerization of this family of cyclic peptides. Studies of peptides 3b−3g show that aromatic residues across from Hao improve folding of the peptide, while studies of peptides 3h−3n indicate that hydrophobic residues at positions R3 and R5 of the heptapeptide sequence are important in oligomerization.

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     University of California, Irvine.

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     University of Texas Health Science Center.

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    In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

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    Experimental procedures and NMR spectra, mass spectra, and HPLC traces for cyclic peptides. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cite this: J. Am. Chem. Soc. 2007, 129, 17, 5558–5569
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