Publications
2004
Poschalko Alexander, Lancelot Nathalie, Marin Julien, Larras Virginie, Limal David, Elbayed Karim, Raya Jesus, Piotto Martial, Briand Jean-Paul, Guichard Gilles, Bianco Alberto
DEUSS: A Perdeuterated Poly(oxyethylene)-Based Resin for Improving HRMAS NMR Studies of Solid-Supported Molecules Article de journal
Dans: Chemistry – A European Journal, vol. 10, no. 18, p. 4532–4537, 2004, ISSN: 0947-6539.
Résumé | Liens | BibTeX | Étiquettes: combinatorial chemistry, I2CT, NMR spectroscopy, oligoureas, Peptides, poly(oxyethylene), Resins, Team-Bianco
@article{poschalko_deuss_2004,
title = {DEUSS: A Perdeuterated Poly(oxyethylene)-Based Resin for Improving HRMAS NMR Studies of Solid-Supported Molecules},
author = {Alexander Poschalko and Nathalie Lancelot and Julien Marin and Virginie Larras and David Limal and Karim Elbayed and Jesus Raya and Martial Piotto and Jean-Paul Briand and Gilles Guichard and Alberto Bianco},
url = {https://chemistry-europe.onlinelibrary.wiley.com/doi/abs/10.1002/chem.200400373},
doi = {10.1002/chem.200400373},
issn = {0947-6539},
year = {2004},
date = {2004-09-01},
urldate = {2020-03-31},
journal = {Chemistry – A European Journal},
volume = {10},
number = {18},
pages = {4532--4537},
abstract = {Abstract A novel resin called DEUSS (perdeuterated poly(oxyethylene)-based solid support) has been prepared by anionic polymerization of deuterated [D4]ethylene oxide, followed by cross-linking with deuterated epichlorohydrin. DEUSS can be suspended in a wide range of solvents including organic and aqueous solutions, in which it displays a high swelling capacity. As measured by proton HRMAS of the swollen polymer, the signal intensity of the oxyethylene protons is reduced by a factor of 110 relative to the corresponding nondeuterated poly(oxyethylene)poly(oxypropylene) (POEPOP) resin, thus facilitating detailed HRMAS NMR studies of covalently linked molecules. This 1H NMR invisible matrix was used for the solid-phase synthesis of peptides, oligoureas, and a series of amides as well as their characterization by HRMAS NMR spectroscopy. On-bead NMR spectra of high quality and with resolution comparable to that of liquid samples were obtained and readily interpreted. The complete absence of the parasite resin signals will be of great advantage, for example, for the optimization of multistep solid-phase stereoselective reactions, and for the conformational study of resin-bound molecules in a large variety of solvents.},
keywords = {combinatorial chemistry, I2CT, NMR spectroscopy, oligoureas, Peptides, poly(oxyethylene), Resins, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
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}
}
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}
}
1992
Wilhelm M. L., Baranowski W., Keith G., Wilhelm F. X.
Rapid transfer of small RNAs from a polyacrylamide gel onto a nylon membrane using a gel dryer Article de journal
Dans: Nucleic Acids Res, vol. 20, no. 15, p. 4106, 1992, (0305-1048 Journal Article).
BibTeX | Étiquettes: &, 5S/*isolation, Acrylic, Human, Nuclear/*isolation, Nylons, purification, Resins, Ribosomal, RNA, Small, Transfer/*isolation, Yeasts/genetics
@article{,
title = {Rapid transfer of small RNAs from a polyacrylamide gel onto a nylon membrane using a gel dryer},
author = { M. L. Wilhelm and W. Baranowski and G. Keith and F. X. Wilhelm},
year = {1992},
date = {1992-01-01},
journal = {Nucleic Acids Res},
volume = {20},
number = {15},
pages = {4106},
note = {0305-1048
Journal Article},
keywords = {&, 5S/*isolation, Acrylic, Human, Nuclear/*isolation, Nylons, purification, Resins, Ribosomal, RNA, Small, Transfer/*isolation, Yeasts/genetics},
pubstate = {published},
tppubtype = {article}
}