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  • 1
    ISSN: 1075-2617
    Keywords: (αMe) amino acids ; CD spectroscopy ; 310-helix ; peptide 3D-structure ; X-ray structure ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The terminally blocked tetrapeptide pBrBz-[D-(αMe)Leu]2-D-(αMe)Val-D-(αMe)Leu-OtBu is folded in the crystal state in a left-handed 310-helical structure stabilized by two consecutive 1 ← 4 C=O⃛H—N intramolecular H-bonds, as determined by X-ray diffraction analysis. A CD study strongly supports the view that this conformation is also that largely prevailing in MeOH solution. A comparison with the published conformation of pBrBz-[D-(αMe)Leu]4-OtBu indicates that incorporation of a single internal β-branched (αMe)Val guest residue into the host homo-tetrapeptide from the γ-branched (αMe)Leu residue is responsible for a dramatic structural perturbation, i.e. an inversion of the 310 screw sense from right to left-handed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 2
    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.
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  • 3
    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.
    Type of Medium: Electronic Resource
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