Two analogs of the ten-amino acid residue, membrane-active lipopeptaibiotic trichogin GA IV, mono-labeled with 4-cyano-α-methyl-L-phenylalanine, a potentially useful fluorescence and IR absorption probe of the local microenvironment, were synthesized by the solid-phase methodology and conformationally characterized. The single modification was incorporated either at the N-terminus (position 1) or near the C-terminus (position 8) of the peptide main chain. In both cases, the replaced amino acid was the equally helicogenic α-aminoisobutyric acid (Aib) residue. We performed a solution conformational analysis by use of FT-IR absorption, CD, and 2D-NMR spectroscopies. The results indicate that both labeled analogs essentially maintain the overall helical propensity of the naturally occurring lipopeptaibiotic. Peptide-membrane interactions were assessed by fluorescence and ATR-IR absorption techniques. Analogies and differences between the two peptides were highlighted. Taken together, our data confirm literature results that some of the spectroscopic parameters of the 4-cyanobenzyl chromophore are sensitive markers of the local microenvironment.

De Zotti, M., Bobone, S., Bortolotti, A., Longo, E., Biondi, B., Peggion, C., et al. (2015). 4-Cyano-α-methyl- l- phenylalanine as a spectroscopic marker for the investigation of peptaibioticmembrane interactions. CHEMISTRY & BIODIVERSITY, 12(4), 513-527 [10.1002/cbdv.201400404].

4-Cyano-α-methyl- l- phenylalanine as a spectroscopic marker for the investigation of peptaibioticmembrane interactions

BOBONE, SARA;BORTOLOTTI, ANNALISA;STELLA, LORENZO
2015-01-01

Abstract

Two analogs of the ten-amino acid residue, membrane-active lipopeptaibiotic trichogin GA IV, mono-labeled with 4-cyano-α-methyl-L-phenylalanine, a potentially useful fluorescence and IR absorption probe of the local microenvironment, were synthesized by the solid-phase methodology and conformationally characterized. The single modification was incorporated either at the N-terminus (position 1) or near the C-terminus (position 8) of the peptide main chain. In both cases, the replaced amino acid was the equally helicogenic α-aminoisobutyric acid (Aib) residue. We performed a solution conformational analysis by use of FT-IR absorption, CD, and 2D-NMR spectroscopies. The results indicate that both labeled analogs essentially maintain the overall helical propensity of the naturally occurring lipopeptaibiotic. Peptide-membrane interactions were assessed by fluorescence and ATR-IR absorption techniques. Analogies and differences between the two peptides were highlighted. Taken together, our data confirm literature results that some of the spectroscopic parameters of the 4-cyanobenzyl chromophore are sensitive markers of the local microenvironment.
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore CHIM/02 - Chimica Fisica
English
L-Phenylalanine, 4-cyano-α-methyl-; Membrane activity; Peptaibols; Solid-phase synthesis
De Zotti, M., Bobone, S., Bortolotti, A., Longo, E., Biondi, B., Peggion, C., et al. (2015). 4-Cyano-α-methyl- l- phenylalanine as a spectroscopic marker for the investigation of peptaibioticmembrane interactions. CHEMISTRY & BIODIVERSITY, 12(4), 513-527 [10.1002/cbdv.201400404].
De Zotti, M; Bobone, S; Bortolotti, A; Longo, E; Biondi, B; Peggion, C; Formaggio, F; Toniolo, C; Dallabona, A; Kaptein, B; Stella, L
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/118190
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