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  • 1
    Electronic Resource
    Electronic Resource
    Hemoprotein Models Based on a Covalent Helix-Heme-Helix Sandwich: 1. Design, Synthesis, and Characterization (1997)
    Weinheim : Wiley-Blackwell
    Chemistry - A European Journal 3 (1997), S. 340-349 
    Details
    ISSN: 0947-6539
    Keywords: helical structures ; heme proteins ; iron ; peptides ; synthesis design ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In this paper we describe the design, synthesis, and spectroscopic characterization of a covalent helix-heme-helix sandwich named FeIII mimochrome I. It contains deuterohemin bound through both propionyl groups to two identical N-and C-terminal protected nonapeptides as α-helical scaffolds. Each peptide moiety bears a His residue in the central position, which acts as axial ligand to the metal ion. The newly developed synthetic strategy is based on a combination of solution and solid-phase methodologies. It represents a powerful method for obtaining a large variety of analogues containing two symmetric or unsymmetric peptide chains covalently bound to the deuteroporphyrin ring. UV/Visible spectroscopic characterization in buffered 2,2,2-trifluoroethanol/water solution proves low-spin bis(his-tidine) iron(III) coordination; circular dichroism (CD) measurements show an α-helical conformation for the peptide moieties. Thus, all the data are in agreement with the designed hypothetical model regarding both the iron(III) coordination and the peptide chain structural organization.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/chem.19970030305
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  • 2
    Electronic Resource
    Electronic Resource
    Hemoprotein Models Based on a Covalent Helix-Heme-Helix Sandwich: 2. Structural Characterization of CoIII Mimochrome I δ and δ Isomers (1997)
    Weinheim : Wiley-Blackwell
    Chemistry - A European Journal 3 (1997), S. 350-362 
    Details
    ISSN: 0947-6539
    Keywords: cobalt ; helical structures ; heme proteins ; NMR spectroscopy ; por-phyrinoids ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: FeIII mimochrome I is the prototype of a new class of hemoprotein models characterized by a covalent helix-heme-helix sandwich. It contains deuterohemin bound through two propionyl groups to two identical N- and C-terminal protected α-helical nonapeptides, each of which bears a His residue (a potential axial lig-and of the iron ion) in the central position. In order to understand better the three-dimensional structure of FeIII mimochrome I and its correlation with spectral properties, we have characterized the fully diamagnetic parent compound CoIII mimochrome I by UV/visible, CD, and NMR spectroscopy, coupled with conformational energy calculations. CoIII mimochrome I is a highly water-soluble compound present in solution as two isomers, which slowly interconvert only at very low pH values. These isomers were isolated and separately characterized. Their UV/visible spectral properties are very similar, while their CD spectral properties differ markedly in both the far UV and Soret regions. The isomers were identified by 1H NMR spectroscopy as diastereomers of the δ and δ type. This is the first example of an accurate three-dimensional structure determination in solution of a hemoprotein mimetic that allows a straightforward correlation between structure and spectral properties.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/chem.19970030306
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  • 3
    Electronic Resource
    Electronic Resource
    Solution and solid state structure of an aib-containing cyclodecapeptide inhibiting the cholate uptake in hepatocytes (1996)
    New York : Wiley-Blackwell
    Biopolymers 40 (1996), S. 465-478 
    Details
    ISSN: 0006-3525
    Keywords: cyclic decapeptides ; cyclolinopeptide A ; x-ray ; nmr ; conformation ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational analysis of synthetic cyclodecapeptide c(Pro-Phe-Phe-Aib-Leu)2 related to the cyclolinopeptide A, in the solid state and solution, has been carried out by x-ray diffraction and nmr spectroscopy. The structure of the monoclinic form obtained from methanol [a = 11.351(5) Å, b = 27.455(2) Å, c = 12.716(8) Å, β = 99.65(3)°; space group P21; Z = 2] shows the presence of six intramolecular NH···CO hydrogen bonds, with formation of four turns (three of type I and one of type III) and two C16 ring structures. All peptide units are trans. The solution structure, as found by nmr, indicates that, at room temperature, the peptide is conformationally homogeneous; the structure determined is perfectly symmetrical and topologically similar to that found in the solid state. The cyclodecapeptide exhibits similar biological activity to cyclolinopeptide A. © 1997 John Wiley & Sons, Inc. Biopoly 40: 465-478, 1996
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Bicyclic peptides as type I/type II β-turn scaffolds (1996)
    New York : Wiley-Blackwell
    Biopolymers 40 (1996), S. 505-518 
    Details
    ISSN: 0006-3525
    Keywords: molecular scaffolds ; β-turn ; tachykinin antagonist ; x-ray ; nmr ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: We recently reported the rational design, synthesis, and structural characterization of the most potent and selective peptide-based neurokinin A antagonist thus far described: cyclo(Met1-Asp2-Trp3-Phe4-Dap5-Leu6)cyclo(2β-5β). Its bicyclic structure is characterized by a type I and a type II two β-turn around Trp3-Phe4 and Leu6-Met1, respectively. In order to understand whether the two different β-turned structures are determined by the bicyclic structure or by the amino acid type at the corner positions, we have synthesized the pseudosymmetrical analogue cyclo(Phe1-Asp2-Trp3-Phe4-Dap5-Trp6)cyclo(2β-5β). The structural characterization in the crystal state and in solution, here reported, gives an experimental evidence that the backbone of the bicyclic structure is a rigid scaffold that can be used to build both a type I and type II β-turn independently from the amino acid composition. © 1997 John Wiley & Sons, Inc. Biopoly 40: 505-518, 1996
    Additional Material: 8 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    Solution conformational preferences of a peptidic analogue of a natural macrolide (1997)
    New York : Wiley-Blackwell
    Biopolymers 42 (1997), S. 349-361 
    Details
    ISSN: 0006-3525
    Keywords: cyclic peptides ; molecular dynamics ; nmr ; conformation ; FK506 ; FK506 binding proteins ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational behavior in solution of a cyclic peptide with sequence cyclo-(Pro1-Pro2-Dab3 (cHexA)ψ[N7HCO]-Leu4ψ[NHCO]-Suc5-Gly6-) has been throughly investigated with the combined use of nmr and molecular dynamic techniques. The compound, which has been modeled to mimic the FK506 macrolide bound to the FK506 binding protein structure, can be considered as a peptidic analogue of the FK506 system.The synthesis was carried out on a phenylacetoamidomethyl resin using an appropriate protocol for the peptide chain elongation. The conformational properties of the cyclic hexapeptide were studied in DMSO and water. The nmr data in DMSO and restrained molecular dynamics simulations show the presence of two contiguous cis peptide bonds involving the -Gly-Pro-Pro- segment. This segment in water exhibits conformational heterogeneity presenting at least two distinct conformational families, characterized the first by cis-cis and the second by a trans-cis Gly-Pro-Pro configuration; the trans-cis isomer was fully characterized. © 1997 John Wiley & Sons, Inc. Biopoly 42: 349-361, 1997
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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