Publications
2003
Rainaldi Mario, Lancelot Nathalie, Elbayed Karim, Raya Jesus, Piotto Martial, Briand Jean-Paul, Kaptein Bernard, Broxterman Quirinus B, Berkessel Albrecht, Formaggio Fernando, Toniolo Claudio, Bianco Alberto
Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from C(alpha)-methyl-leucine Article de journal
Dans: Organic & Biomolecular Chemistry, vol. 1, no. 11, p. 1835–1837, 2003, ISSN: 1477-0520.
Résumé | Liens | BibTeX | Étiquettes: biomolecular, I2CT, Leucine, Nuclear Magnetic Resonance, Oligopeptides, Protein Structure, Resins, Secondary, Synthetic, Team-Bianco
@article{rainaldi_conformational_2003,
title = {Conformational analysis by HRMAS NMR spectroscopy of resin-bound homo-peptides from C(alpha)-methyl-leucine},
author = {Mario Rainaldi and Nathalie Lancelot and Karim Elbayed and Jesus Raya and Martial Piotto and Jean-Paul Briand and Bernard Kaptein and Quirinus B Broxterman and Albrecht Berkessel and Fernando Formaggio and Claudio Toniolo and Alberto Bianco},
doi = {10.1039/b303193d},
issn = {1477-0520},
year = {2003},
date = {2003-06-01},
journal = {Organic & Biomolecular Chemistry},
volume = {1},
number = {11},
pages = {1835--1837},
abstract = {A series of [L-(alphaMe)Leu]n (n = 1-5) homo-peptides have been covalently linked to Tentagel and POEPOP resins and submitted to a conformational study using HRMAS NMR spectroscopy. Whereas the mono- and dipeptide are mainly fully-extended, stable 3(10)-helical structures are formed beginning from the trimer.},
keywords = {biomolecular, I2CT, Leucine, Nuclear Magnetic Resonance, Oligopeptides, Protein Structure, Resins, Secondary, Synthetic, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Pantarotto Davide, Partidos Charalambos D, Graff Roland, Hoebeke Johan, Briand Jean-Paul, Prato Maurizio, Bianco Alberto
Synthesis, structural characterization, and immunological properties of carbon nanotubes functionalized with peptides Article de journal
Dans: Journal of the American Chemical Society, vol. 125, no. 20, p. 6160–6164, 2003, ISSN: 0002-7863.
Résumé | Liens | BibTeX | Étiquettes: B-Lymphocyte, biomolecular, Capsid Proteins, carbon, Chromatography, Epitopes, Foot-and-Mouth Disease Virus, High Pressure Liquid, I2CT, nanotechnology, Nanotubes, Nuclear Magnetic Resonance, Peptide Fragments, Team-Bianco
@article{pantarotto_synthesis_2003,
title = {Synthesis, structural characterization, and immunological properties of carbon nanotubes functionalized with peptides},
author = {Davide Pantarotto and Charalambos D Partidos and Roland Graff and Johan Hoebeke and Jean-Paul Briand and Maurizio Prato and Alberto Bianco},
doi = {10.1021/ja034342r},
issn = {0002-7863},
year = {2003},
date = {2003-05-01},
journal = {Journal of the American Chemical Society},
volume = {125},
number = {20},
pages = {6160--6164},
abstract = {Carbon nanotubes (NTs) are becoming highly attractive molecules for applications in medicinal chemistry. The main problem of insolubility in aqueous media has been solved by developing a synthetic protocol that allows highly water-soluble carbon NTs to be obtained. As a result, biologically active peptides can be easily linked through a stable covalent bond to carbon NTs. We have demonstrated that a bound peptide from the foot-and-mouth disease virus, corresponding to the 141-159 region of the viral envelope protein VP1, retained the structural integrity and was recognized by monoclonal and polyclonal antibodies. In addition, this peptide-NT conjugate is immunogenic, eliciting antibody responses of the right specificity. Such a system could be greatly advantageous for diagnostic purposes and could find future applications in vaccine delivery.},
keywords = {B-Lymphocyte, biomolecular, Capsid Proteins, carbon, Chromatography, Epitopes, Foot-and-Mouth Disease Virus, High Pressure Liquid, I2CT, nanotechnology, Nanotubes, Nuclear Magnetic Resonance, Peptide Fragments, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Lancelot Nathalie, Elbayed Karim, Raya Jésus, Piotto Martial, Briand Jean-Paul, Formaggio Fernando, Toniolo Claudio, Bianco Alberto
Characterization of the 310-helix in model peptides by HRMAS NMR spectroscopy Article de journal
Dans: Chemistry (Weinheim an Der Bergstrasse, Germany), vol. 9, no. 6, p. 1317–1323, 2003, ISSN: 0947-6539.
Résumé | Liens | BibTeX | Étiquettes: biomolecular, Fourier Transform Infrared, I2CT, Nuclear Magnetic Resonance, Peptides, Protein Conformation, spectroscopy, Team-Bianco
@article{lancelot_characterization_2003,
title = {Characterization of the 310-helix in model peptides by HRMAS NMR spectroscopy},
author = {Nathalie Lancelot and Karim Elbayed and Jésus Raya and Martial Piotto and Jean-Paul Briand and Fernando Formaggio and Claudio Toniolo and Alberto Bianco},
doi = {10.1002/chem.200390151},
issn = {0947-6539},
year = {2003},
date = {2003-03-01},
journal = {Chemistry (Weinheim an Der Bergstrasse, Germany)},
volume = {9},
number = {6},
pages = {1317--1323},
abstract = {A tetra- and a hepta-homopeptide from the C(alpha)-tetrasubstituted Aib (alpha-aminoisobutyric acid) residue were covalently linked to the POEPOP resin by the fragment-condensation approach. The conformational preferences of the two model peptides were determined for the first time on a solid support by means of high-resolution magic angle spinning NMR spectroscopy. The results obtained indicate that the Aib homopeptides adopt a regular 3(10)-helical structure even when they are covalently bound to a polymeric matrix, and thus confirm the remarkable conformational stability of the peptides rich in this amino acid. An ATR-FTIR spectroscopic investigation, performed in parallel, also confirmed that these polymer-bound peptides do indeed adopt a helical conformation. The results of this study open the possibility to exploit the peptide-resin conjugates based on C(alpha)-tetrasubstituted alpha-amino acids as helpful, structurally organized templates in molecular recognition studies or as catalysts in asymmetric synthesis.},
keywords = {biomolecular, Fourier Transform Infrared, I2CT, Nuclear Magnetic Resonance, Peptides, Protein Conformation, spectroscopy, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
2002
Raya Jésus, Bianco Alberto, Furrer Julien, Briand Jean-Paul, Piotto Martial, Elbayed Karim
Proton dipolar recoupling in resin-bound peptides under high-resolution magic angle spinning Article de journal
Dans: Journal of Magnetic Resonance (San Diego, Calif.: 1997), vol. 157, no. 1, p. 43–51, 2002, ISSN: 1090-7807.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence, biomolecular, Foot-and-Mouth Disease Virus, I2CT, Nuclear Magnetic Resonance, Peptides, Plant, Resins, Team-Bianco
@article{raya_proton_2002,
title = {Proton dipolar recoupling in resin-bound peptides under high-resolution magic angle spinning},
author = {Jésus Raya and Alberto Bianco and Julien Furrer and Jean-Paul Briand and Martial Piotto and Karim Elbayed},
doi = {10.1006/jmre.2002.2573},
issn = {1090-7807},
year = {2002},
date = {2002-07-01},
journal = {Journal of Magnetic Resonance (San Diego, Calif.: 1997)},
volume = {157},
number = {1},
pages = {43--51},
abstract = {Rotational resonance and radiofrequency-driven dipolar recoupling (RFDR) experiments have been used to recover the weak proton dipolar interaction present in peptides bound to swollen resins spun at the magic angle. The intensity of the correlation peaks obtained using these sequences is shown to be significantly stronger than the one obtained using the classical NOESY experiment. In addition, it is found that during the relatively long mixing times required to transfer magnetization in such soft materials, the RFDR sequence also achieves magnetization transfer via the scalar J-coupling.},
keywords = {Amino Acid Sequence, biomolecular, Foot-and-Mouth Disease Virus, I2CT, Nuclear Magnetic Resonance, Peptides, Plant, Resins, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
2001
Furrer J, Piotto M, Bourdonneau M, Limal D, Guichard G, Elbayed K, Raya J, Briand J P, Bianco A
Evidence of secondary structure by high-resolution magic angle spinning NMR spectroscopy of a bioactive peptide bound to different solid supports Article de journal
Dans: Journal of the American Chemical Society, vol. 123, no. 18, p. 4130–4138, 2001, ISSN: 0002-7863.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence, biomolecular, Capsid, Capsid Proteins, Epitopes, I2CT, Molecular Sequence Data, Nuclear Magnetic Resonance, Peptide Fragments, Plant, Protein Structure, Resins, Secondary, Solvents, Team-Bianco
@article{furrer_evidence_2001,
title = {Evidence of secondary structure by high-resolution magic angle spinning NMR spectroscopy of a bioactive peptide bound to different solid supports},
author = {J Furrer and M Piotto and M Bourdonneau and D Limal and G Guichard and K Elbayed and J Raya and J P Briand and A Bianco},
doi = {10.1021/ja003566w},
issn = {0002-7863},
year = {2001},
date = {2001-01-01},
journal = {Journal of the American Chemical Society},
volume = {123},
number = {18},
pages = {4130--4138},
abstract = {The structure of the 19-amino acid peptide epitope, corresponding to the 141-159 sequence of capsid viral protein VP1 of foot-and-mouth disease virus (FMDV), bound to three different resins, namely, polystyrene-MBHA, PEGA, and POEPOP, has been determined by high-resolution magic angle spinning (HRMAS) NMR spectroscopy. A combination of homonuclear and heteronuclear bidimensional experiments was used for the complete peptide resonance assignment and the qualitative characterization of the peptide folding. The influence of the chemicophysical nature of the different polymers on the secondary structure of the covalently attached FMDV peptide was studied in detail. In the case of polystyrene-MBHA and polyacrylamide-PEGA resins, the analysis of the 2D spectra was hampered by missing signals and extensive overlaps, and only a propensity toward a peptide secondary structure could be derived from the assigned NOE correlations. When the FMDV peptide was linked to the polyoxyethylene-based POEPOP resin, it was found to adopt in dimethylformamide a helical conformation encompassing the C-terminal domain from residues 152 to 159. This conformation is very close to that of the free peptide previously analyzed in 2,2,2-trifluoroethanol. Our study clearly demonstrates that a regular helical structure can be adopted by a resin-bound bioactive peptide. Moreover, a change in the folding was observed when the same peptide-POEPOP conjugate was swollen in aqueous solution, displaying the same conformational features as the free peptide in water. The possibility of studying solid-supported ordered secondary structures by the HRMAS NMR technique in a wide range of solvents can be extended either to other biologically relevant peptides and proteins or to new synthetic oligomers.},
keywords = {Amino Acid Sequence, biomolecular, Capsid, Capsid Proteins, Epitopes, I2CT, Molecular Sequence Data, Nuclear Magnetic Resonance, Peptide Fragments, Plant, Protein Structure, Resins, Secondary, Solvents, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}