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Functionalised mesoporous silica: a good opportunity for controlled peptide oligomerisation

Authors :
Christine Enjalbal
Muriel Amblard
Robert J. P. Corriu
Luc Brunel
Ahmad Mehdi
Gilles Subra
Jean Martinez
Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM)
Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)
Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier (ICGM ICMMM)
Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut de Chimie du CNRS (INC)
Source :
Journal of Materials Chemistry, Journal of Materials Chemistry, Royal Society of Chemistry, 2011, 21, pp.6321-6326. ⟨10.1039/cOjm04492j⟩
Publication Year :
2011
Publisher :
HAL CCSD, 2011.

Abstract

International audience; 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.

Details

Language :
English
ISSN :
09599428 and 13645501
Database :
OpenAIRE
Journal :
Journal of Materials Chemistry, Journal of Materials Chemistry, Royal Society of Chemistry, 2011, 21, pp.6321-6326. ⟨10.1039/cOjm04492j⟩
Accession number :
edsair.doi.dedup.....64b19727938ac6cab82d9545ef3aa160
Full Text :
https://doi.org/10.1039/cOjm04492j⟩