References of "Vandevenne, Marylène"
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See detailHow to build a biological linker dedicated to the engineering of novel drug delivery systems
Crasson, Oscar ULg; Galleni, Moreno ULg; Parente, Raffaella et al

Poster (2014, May 15)

Nowadays, chemical linkages are widely used in industry to coat bioactive molecules on biocompatible supports. However, some issues inherent to the linkage procedure remain. For example, chemical ... [more ▼]

Nowadays, chemical linkages are widely used in industry to coat bioactive molecules on biocompatible supports. However, some issues inherent to the linkage procedure remain. For example, chemical reactions often damage the structure and therefore the activity of the immobilized molecules. In this work, we propose the use of a human chitin binding domain (ChBD) to immobilized bioactive molecules on a polysaccharide-based surface. ChBD belongs to the human chitinase called chitotriosidase and was shown to interact specifically with chitin and chitooligomers. Using molecular biology and protein engineering, we have developped of a new biological tool based on the hybrid protein technology. In this technology, we can create chimeric proteins that have the ability to bind polysaccharidic supports thanks to their binding domain that can be covalently linked with any bioactive molecule that can confer prophylactic or therapeutic activities. In this study, we have successfully shown that we can use the chitin binding domain (ChBD) from the human chitotriosidase as a biological linker dedicated to the engineering of novel drug delivery systems containing chitin or other analogous polysaccharides. [less ▲]

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See detailThe Bacillus licheniformis BlaP beta-lactamase as a model protein scaffold to study the insertion of protein fragments.
Vandevenne, Marylène ULg; Filée, Patrice ULg; Scarafone, Natacha ULg et al

in Protein Science : A Publication of the Protein Society (2007), 16(10), 2260-71

Using genetic engineering technologies, the chitin-binding domain (ChBD) of the human macrophage chitotriosidase has been inserted into the host protein BlaP, a class A beta-lactamase produced by Bacillus ... [more ▼]

Using genetic engineering technologies, the chitin-binding domain (ChBD) of the human macrophage chitotriosidase has been inserted into the host protein BlaP, a class A beta-lactamase produced by Bacillus licheniformis. The product of this construction behaved as a soluble chimeric protein that conserves both the capacity to bind chitin and to hydrolyze beta-lactam moiety. Here we describe the biochemical and biophysical properties of this protein (BlaPChBD). This work contributes to a better understanding of the reciprocal structural and functional effects of the insertion on the host protein scaffold and the heterologous structured protein fragments. The use of BlaP as a protein carrier represents an efficient approach to the functional study of heterologous protein fragments. [less ▲]

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