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| Content Provider | Royal Society of Chemistry (RSC) |
|---|---|
| Author | Dumy, Pascal Renaudet, Olivier Coche-Guérente, Liliane Wilczewski, Marie Heyden, Angéline Van Labbé, Pierre |
| Copyright Year | 2008 |
| Abstract | The investigation of recognition events between carbohydrates and proteins, especially the understanding of how spatial factors and binding avidity are correlated, remains a great interest for glycobiology. In this context we have investigated by nanogravimetry (QCM-D) and surface plasmon resonance (SPR), the kinetics and thermodynamics of the interaction between concanavalin A (Con A) and various neoglycopeptide ligands of low molecular weight. Regioselectively addressable functionalized templates (RAFT) have been used as scaffolds for the design of multivalent neoglycopeptides bearing thiol or biotin functions for their anchoring on transducer surfaces. Although these multivalent neoglycopeptide ligands cannot span multiple binding sites within the same Con A protein, they have increased activities relative to their monovalent counterpart. Our results emphasize that the multivalent RAFT ligands function by clustering several lectins, which leads to enhanced affinities. |
| Starting Page | 1114 |
| Ending Page | 1122 |
| Page Count | 9 |
| File Format | HTM / HTML PDF |
| ISSN | 14770520 |
| Volume Number | 6 |
| Issue Number | 6 |
| Journal | Organic & Biomolecular Chemistry |
| DOI | 10.1039/b716214f |
| Language | English |
| Publisher | Royal Society of Chemistry |
| Access Restriction | Open |
| Subject Keyword | Signal transduction Thiol Glycobiology Quartz crystal microbalance with dissipation monitoring Surface plasmon resonance Biotin Surface plasmon Concanavalin A Protein |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Biochemistry Physical and Theoretical Chemistry |
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