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

Autor: Bernard Kaptein, Barbara Biondi, Marta De Zotti, Edoardo Longo, Sara Bobone, Claudio Toniolo, Cristina Peggion, Andrea Dalla Bona, Fernando Formaggio, Annalisa Bortolotti, Lorenzo Stella
Rok vydání: 2014
Předmět:
Aminoisobutyric Acids
Magnetic Resonance Spectroscopy
Solid-phase synthesis
Stereochemistry
Phenylalanine
Molecular Conformation
L-Phenylalanine
4-cyano-α-methyl
Membrane activity
Peptaibols
Bioengineering
Peptide
Biochemistry
INFRARED-SPECTROSCOPY
TRICHOGIN GA-IV
2-CHLOROTRITYL CHLORIDE RESIN
ALPHA-AMINO-ACIDS
SYNTHETIC ANALOGS
CONFORMATIONAL-ANALYSIS
ANTIMICROBIAL PEPTIDES
POLYPEPTIDE HELICES
ATOMIC-RESOLUTION
LIPID-MEMBRANES
Residue (chemistry)
Lipopeptides
Nitriles
Spectroscopy
Fourier Transform Infrared
4-cyano-α-methyl
Molecular Biology
4-cyano--methyl
Solid-Phase Synthesis Techniques
Settore CHIM/02 - Chimica Fisica
chemistry.chemical_classification
Chemistry
Circular Dichroism
Cell Membrane
General Chemistry
General Medicine
L-Phenylalanine
Chromophore
Fluorescence
Amino acid
Molecular Medicine
Spectrophotometry
Ultraviolet
Peptides
Zdroj: Chemistry & biodiversity
12 (2015): 513–527. doi:10.1002/cbdv.201400404
info:cnr-pdr/source/autori:De Zotti, Marta; Bobone, Sara; Bortolotti, Annalisa; Longo, Edoardo; Biondi, Barbara; Peggion, Cristina; Formaggio, Fernando; Toniolo, Claudio; Dalla Bona, Andrea; Kaptein, Bernard; Stella, Lorenzo/titolo:4-Cyano-alpha-methyl-L-phenylalanine as a Spectroscopic Marker for the Investigation of Peptaibiotic-Membrane Interactions/doi:10.1002%2Fcbdv.201400404/rivista:Chemistry & biodiversity (Print)/anno:2015/pagina_da:513/pagina_a:527/intervallo_pagine:513–527/volume:12
ISSN: 1612-1880
DOI: 10.1002/cbdv.201400404
Popis: 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.
Databáze: OpenAIRE
Externí odkaz: