AMBLARD Muriel
Fonction : Directeur de recherche
Thème de Recherche: Chimie des Acides Aminés, Peptides, Hétérocycles, Chimie Sup (responsable de)
muriel.amblard
univ-montp1.fr
0411759605
Bureau: 336
Dernieres Publications:
|
|
Functionalised mesoporous silica: a good opportunity for controlled peptide oligomerisation 
Auteur(s): SUBRA G., Mehdi Ahmad, ENJALBAL C., AMBLARD M., BRUNEL L., Corriu Robert, MARTINEZ J.
(Article) Publié:
Journal of Materials Chemistry, vol. 21 (2011) p.6321-6326
Ref HAL: hal-00586041_v1
DOI: 10.1039/cOjm04492j
Résumé: In this paper, mesoporous organosilicas functionalised with aminopropyl groups have been successfully used for peptide oligomerisation. For this purpose, three mesoporous silica SBA-15 type containing different amounts of aminopropyl groups were prepared by direct synthesis and using 3- tert-butyloxycarbonylamino propyltriethoxysilane. Thanks to amino groups and under well selected experimental conditions, amino acids N-carboxyanhydride-polymerisation has been achieved within the pores with control of the physical properties of peptide functionalised hybrid materials. NCA of alanine, side chain protected glutamic acid and methionine were used for this study. For the first time, direct LDI-MS analysis was successfully performed on the resulting covalently bound supported oligomers. To demonstrate the potential application of this class of hybrid bio-organic-inorganic material as supported catalysts, one of the methionine-functionalized OMSs was used to promote disulfide bond formation in a model peptide.
|
|
|
|
Solid-Phase Cross-Linking (SPCL): A new tool for protein structure studies
Auteur(s): PARAMELLE D., ENJALBAL C., AMBLARD M., Forest Eric, Heymann Michaël, CANTEL S., Geourjon Christophe, MARTINEZ J., SUBRA G.
(Article) Publié:
Proteomics, vol. 11 (2011) p.1277-1286
Ref HAL: hal-00580912_v1
DOI: 10.1002/pmic.201000029
Résumé: A wide range of chemical reagents are available to study the protein-protein interactions or protein structures. After reaction with such chemicals, covalently modified proteins are digested, resulting in shorter peptides that are analyzed by mass spectrometry (MS). Used especially when NMR of X-ray data are lacking, this methodology requires the identification of modified species carrying relevant information, among the unmodified peptides. To overcome the drawbacks of existing methods, we propose a more direct strategy relying on the synthesis of solid-supported cleavable monofunctional reagents and cross-linkers that react with proteins and that selectively release, after protein digestion and washings, the modified peptide fragments ready for MS analysis. Using this Solid-Phase Cross-Linking (SPCL) strategy, only modified sequences are analyzed and consistent data can be easily obtained since the signals of interest are not masked or suppressed by over-represented unmodified materials.
|
|
|
|
Easy Synthesis and Ring-Opening Polymerization of 5-Z-Amino-d-valerolactone: New Degradable Amino-Functionalized (Co)polyesters
Auteur(s): BLANQUER S., TAILHADES J., DARCOS V., AMBLARD M., MARTINEZ J., AMBLARD M., NOTTELET B. , COUDANE J.
(Article) Publié:
Journal of Polymer Science Part A Polymer Chemistry / JOURNAL OF POLYMER SCIENCE PART A-POLYMER CHEMISTRY, vol. 48 (2010) p.5891-5898
Ref HAL: hal-00536858_v1
DOI: 10.1002/pola.24400
Résumé: Novel 5-Z-amino-d-valerolactone (5-NHZ-VL) was synthesized with aim to prepare degradable polyesters and copolyesters having amino pendant groups. Following a straightforward and efficient synthetic pathway, 5-NHZ-VL was obtained in only two steps and up to 50 % yield. The monomer was fully characterized by 1H NMR, 13C NMR, ESI mass spectrometry and HPLC. Various conventional conditions were tested for this lactone ring opening polymerization and led to the novel corresponding poly(5-NHZ-VL) (Mn = 7000 g/mol ; PD = 1.2). Following this homopolymerization, 5-NHZ-VL was copolymerized with e-caprolactone to generate a family of copolyesters with an amino-group content ranging from 10 to 80 %. Finally, the polyelectrolyte poly(5-NH3+-VL) was recovered by removal of the protecting group under acidic conditions and integrity of the polyester backbone was confirmed by 1H NMR.
|
|
|
|
Synthesis of Peptide Alcohols on the Basis of an O-N Acyl-Transfer Reaction
Auteur(s): TAILHADES J., Gidel M. A., Grossi B., Lecaillon J., BRUNEL L., SUBRA G., MARTINEZ J., AMBLARD M.
(Article) Publié:
Angewandte Chemie International Edition, vol. 49 (2010) p.117-120
Commentaires: 543ZI Times Cited:0 Cited References Count:38
|
Plus...
Calcpeg
Chemaztech
