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Molecular recognition of carbohydrates by acyclic receptors employing noncovalent interactions
Abstract
Artificial carbohydrate receptors using noncovalent interactions for sugar binding provide valuable model systems to study the underlying principles of carbohydrate-based molecular recognition processes. In addition, well-designed artificial receptors may serve as a basis for the development of saccharide sensors or therapeutics that intervene in biologically important carbohydrate recognitions. Several different strategies have been employed for the design of such synthetic systems. The main focus of this tutorial review is on the carbohydrate binding capabilities of receptors possessing an acyclic structure and employing noncovalent interactions for sugar binding. The acyclic scaffold provides simplicity in the synthetic plan for many modifications of the receptor structure, supplying a base for systematic studies toward recognition motifs for carbohydrates. The review covers both some earlier examples and newer developments in this field.
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Citations
Cited by
Takahashi, O., Kohno, Y., & Nishio, M. (2010) · Chemical Reviews · doi:10.1021/cr100072x · Cited by 583
Experimental Binding Energies in Supramolecular Complexes
Biedermann, F., & Schneider, H.-J. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00583 · Cited by 554
Carbohydrate–Aromatic Interactions
Asensio, J. L., Ardá, A., Cañada, F. J., & Jiménez-Barbero, J. (2013) · Accounts of Chemical Research · doi:10.1021/ar300024d · Cited by 488
Solís, D., Bovin, N. V., Davis, A. P., Jiménez-Barbero, J., Romero, A., Roy, R., Smetana, K., & Gabius, H.-J. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.03.016 · Cited by 222
Metadata
- Authors
- Mazik, M.
- Venue
- Chemical Society Reviews
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2009
- Volume
- 38
- Issue
- 4
- Pages
- 935
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2018496680
- Cited by
- 249
- References
- 0
- FWCI
- 0.64
- Type
- journal article
- Language
- en
- Open access
- closed
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