344608-07-7Relevant academic research and scientific papers
Peptaibolin: Synthesis, 3D-structure, and membrane modifying properties of the natural antibiotic and selected analogues
Crisma,Barazza,Formaggio,Kaptein,Broxterman,Kamphuis,Toniolo
, p. 2813 - 2825 (2001)
We synthesized by solution methods and fully characterized the naturally occurring, tetrapeptide antibiotic peptaibolin and selected analogues with replacements at the N- and C-terminal groups and the Cα-tetrasubstituted α-amino acids. The preferred conformation of all of the peptides was assessed in solution by using FT-IR absorption and 1H NMR techniques. Results of the X-ray diffraction analyses of peptaibolin itself and three analogues are also presented. Permeability measurements of such multiple turn forming, very short peptides indicate that peptaibolin is devoid of membrane activity because a lipoyl N-terminal blocking group is an essential requisite.
Role of secondary structure in the asymmetric acylation reaction catalyzed by peptides based on chiral Cα-tetrasubstituted α-amino acids
Formaggio, Fernando,Barazza, Alessandra,Bertocco, Andrea,Toniolo, Claudio,Broxterman, Quirinus B.,Kaptein, Bernard,Brasola, Elena,Pengo, Paolo,Pasquato, Lucia,Scrimin, Paolo
, p. 3849 - 3856 (2007/10/03)
In a recent series of papers, Miller and co-workers were able to show that His(π-Me)-based, terminally protected peptides are potent catalysts of the asymmetric acyl transfer reaction, useful for the kinetic resolution of alcohols. In a structure-supporting solvent, one of the most active compounds, an Aib-containing tetrapeptide, is folded in a doubly intramolecularly H-bonded β-hairpin motif incorporating a type-II′ β-turn conformation. In this work, we have expanded the study of the Miller tetrapeptide by examining a set of analogues and shorter sequences (dipeptide amides), characterized by chiral Cα-tetrasubstituted α-amino acids of diverging bulkiness and optical configuration. Peptide synthesis in solution, conformational analysis by FT-IR absorption and 1H NMR techniques, and screening of catalytic activity as well have been performed. Our results confirm the close relationship between the β-hairpin 3D-structure and the catalytic activity of the peptides. A tetrapeptide analogue slightly more selective than the Miller compound has been found. However, the terminally protected, industrially more appealing, dipeptide amides are poorly effective.
