http://www.cnr.it/ontology/cnr/individuo/prodotto/ID287583
Solution Synthesis, Conformational Analysis, and Antimicrobial Activity of Three Alamethicin F50/5 Analogs Bearing a Trifluoroacetyl Label (Articolo in rivista)
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- Solution Synthesis, Conformational Analysis, and Antimicrobial Activity of Three Alamethicin F50/5 Analogs Bearing a Trifluoroacetyl Label (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/cbdv.201300394 (literal)
- Alternative label
De Zotti, Marta; Ballano, Gema; Jost, Micha; Salnikov, Evgeniy S.; Bechinger, Burkhard; Oancea, Simona; Crisma, Marco; Toniolo, Claudio; Formaggio, Fernando (2014)
Solution Synthesis, Conformational Analysis, and Antimicrobial Activity of Three Alamethicin F50/5 Analogs Bearing a Trifluoroacetyl Label
in Chemistry & biodiversity (Print)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- De Zotti, Marta; Ballano, Gema; Jost, Micha; Salnikov, Evgeniy S.; Bechinger, Burkhard; Oancea, Simona; Crisma, Marco; Toniolo, Claudio; Formaggio, Fernando (literal)
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- Consiglio Nazionale delle Ricerche (CNR); University of Padova; Centre National de la Recherche Scientifique (CNRS); Lucian Blaga University of Sibiu (literal)
- Titolo
- Solution Synthesis, Conformational Analysis, and Antimicrobial Activity of Three Alamethicin F50/5 Analogs Bearing a Trifluoroacetyl Label (literal)
- Abstract
- We prepared, by solution-phase methods, and fully characterized three analogs of the membrane-active peptaibiotic alamethicin F50/5, bearing a single trifluoroacetyl (Tfa) label at the N-terminus, at position 9 (central region) or at position 19 (C-terminus), and with the three Gln at positions 7, 18, and 19 replaced by Glu(OMe) residues. To add the Tfa label at position 9 or 19, a -trifluoroacetylated ,-diaminobutyric acid (Dab) residue was incorporated as a replacement for the original Val(9) or Glu(OMe)(19) amino acid. We performed a detailed conformational analysis of the three analogs (using FT-IR absorption, CD, 2D-NMR, and X-ray diffraction), which clearly showed that Tfa labeling does not introduce any dramatic backbone modification in the predominantly -helical structure of the parent peptaibiotic. The results of an initial solid-state F-19-NMR study on one of the analogs favor the conclusion that the Tfa group is a very promising reporter for the analysis of peptaibioticmembrane interactions. Finally, we found that the antimicrobial activities of the three newly synthesized analogs depend on the position of the Tfa label in the peptide sequence. (literal)
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