A Potent Cyclolinopeptide A Analogue: Solid State and Solution Conformation of cyclo[Pro-Phe-Phe-Ala-Glu(OtBu)]2

Giancarlo Zanotti, Annamaria Maione, Filomena Rossi, Michele Saviano, Marta Filizola, Benedetto Di Blasio, Carlo Pedone, Teodorico Tancredi, Gabriella Saviano

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10 Scopus citations

Abstract

The conformational analysis of cyclo[Pro-Phe-Phe-Ala-Glu(OtBu)]2, in the solid state and in solution, has been carried out by X-ray diffraction and NMR spectroscopy. The structure of the orthorhombic form obtained from dioxane-water-acetonitrile mixture [a = 9,994(1) Å,b = 21.846(5) Å, c = 37.357(9) Å, space group P212121; Z = 4] shows the presence of four intramolecular NH–CO hydrogen bonds, with formation of two β turns (one of type I and one of type II) and two C14 ring structures. All peptide units are trans. The solution structure, as determined 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.

Original languageEnglish
Pages (from-to)8651-8658
Number of pages8
JournalJournal of the American Chemical Society
Volume117
Issue number33
DOIs
StatePublished - 1995
Externally publishedYes

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