http://www.cnr.it/ontology/cnr/individuo/prodotto/ID188637
Synthesis and preliminary conformational analysis of TOAC spin-labeled analogues of the medium-length peptaibiotic tylopeptin B (Articolo in rivista)
- Type
- Label
- Synthesis and preliminary conformational analysis of TOAC spin-labeled analogues of the medium-length peptaibiotic tylopeptin B (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/psc.1413 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Marina Gobbo; Elisabetta Merli; Barbara Biondi; Simona Oancea; Antonio Toffoletti; Fernando Formaggio; Claudio Toniolo (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1. Univ Padua, Dept Chem Sci, ICB Padova Unit, CNR, I-35131 Padua, Italy
2. Univ Lucian Blaga Sibiu, Dept Biochem & Toxicol, Sibiu 550012, Romania (literal)
- Titolo
- Synthesis and preliminary conformational analysis of TOAC spin-labeled analogues of the medium-length peptaibiotic tylopeptin B (literal)
- Abstract
- A set of analogues of the 14-residue peptaibol tylopeptin B, containing the stable free-radical 4-amino-1-oxyl-2,2,6,6,-tetramethylpiperidine-4-carboxylic acid (TOAC) at one or two selected positions, was synthesized by the solid-phase methodology. A solution conformational analysis performed by FTIR absorption and CD suggests that, in membrane-mimicking solvents, the labeled tylopeptin B analogues preserve the helical propensity of the parent peptide, with a preference for the a-helix or the 310-helix type depending upon the nature of the solvent. In aqueous environment, the spin-labeled analogues present a higher content of helical conformation as a consequence of the strong helix promoter effect of the conformationally constrained TOAC residue. We observed a progressive increase of the quenching effect of the nitroxyl radical on the fluorescence of the N-terminal tryptophan as TOAC replaces the Aib residue at positions 13, 8, and 4, respectively. A membrane permeabilization assay performed on two selected analogues, TOAC8- and TOAC13-tylopeptin B, showed that the labeled peptides exhibit membrane-modifying properties comparable with those of the natural peptaibiotic. We conclude that our TOAC paramagnetic analogues of tylopeptin B are good models for a detailed ESR investigation of the mechanism of membrane permeabilization induced by medium-length peptaibiotics. (literal)
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