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Recent Trends in Glycodendrimer Syntheses and Applications
Abstract
Carbohydrate protein interactions are at the front of several biological interactions spanning from cell growth and differentiation, cell signaling, apoptosis, cancer, and microbial infections. Classical medicinal glycochemistry has so far concentrated on designing glycosyl transferase and glycohydrolase inhibitors for which only handful candidates have emerged. Added to the complexity of drug resistances, drugs in development have rapidly witnessed this limitation as well. New approaches are therefore highly encouraged. Amongst these, blocking pathogen adhesions to host tissues as an early preventive mechanism is a foreseeable potentiality. It has the clear advantage that the pathogens are unlikely to mutate their anchoring motifs without upsetting their own binding to host tissues. An added dilemma is that these binding interactions are usually too weak to provide suitable drug candidates. As a consequence, the community has successfully come up with multivalent glycoconjugates having greatly enhanced avidity. An alternative strategy in which both monovalent ligands as well as the multivalent scaffolds undergoing QSAR improvement is thus suggested. This review will highlight recent trends toward the design of multivalent glycodendrimers and their biological applications.
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Cited by
Dendrimers Derived from 1 → 3 Branching Motifs
Newkome, G. R., & Shreiner, C. (2010) · Chemical Reviews · doi:10.1021/cr900341m · Cited by 347
Percec, V., Leowanawat, P., Sun, H.-J., Kulikov, O., Nusbaum, C. D., Tran, T. M., Bertin, A., Wilson, D. A., Peterca, M., Zhang, S., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja403323y · Cited by 310
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Metadata
- Authors
- Chabre, Y., & Roy, R.
- Venue
- Current Topics in Medicinal Chemistry
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2008-09-01
- Volume
- 8
- Issue
- 14
- Pages
- 1237-1285
- ISSN
- 1568-0266 (ISSN-L)
- OpenAlex
- W2083174947
- Cited by
- 213
- References
- 0
- FWCI
- 10.73
- Type
- journal article
- Language
- en
- Open access
- closed
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