Synthesis of high-affinity, hydrophobic monosaccharide derivatives and study of their interaction with concanavalin A, the pea, the lentil, and fava bean lectins
dc.contributor.author | Loganathan, Duraikkannu | en_US |
dc.contributor.author | Osborne, Scott E. | en_US |
dc.contributor.author | Glick, Gary D. | en_US |
dc.contributor.author | Goldstein, Irwin J. | en_US |
dc.date.accessioned | 2006-04-10T14:58:29Z | |
dc.date.available | 2006-04-10T14:58:29Z | |
dc.date.issued | 1992-12 | en_US |
dc.identifier.citation | Loganathan, Duraikkannu, Osborne, Scott E., Glick, Gary D., Goldstein, Irwin J. (1992/12)."Synthesis of high-affinity, hydrophobic monosaccharide derivatives and study of their interaction with concanavalin A, the pea, the lentil, and fava bean lectins." Archives of Biochemistry and Biophysics 299(2): 268-274. <http://hdl.handle.net/2027.42/29695> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DPC414-1JN/2/6a5f5855552be73412f7533b038ca91d | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/29695 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1444465&dopt=citation | en_US |
dc.description.abstract | Concanavalin A (Con A) and agglutinins from the pea (PSA), lentil (LCH), and fava bean (VFA) constitute a group of -mannose/-glucose binding legume lectins. In addition to their sugar binding specificity, these lectins also contain sites that bind hydrophobic ligands. The present study explores a class of nonpolar binding sites reportedly present adjacent to the carbohydrate binding site in PSA, LCH, and VFA. A series of 2-O- and 3-O-substituted nitrobenzoyl and nitrobenzyl derivatives of methyl [alpha]--glucopyranoside and methyl [alpha]--mannopyranoside were synthesized. Evaluation of their binding to Con A, PSA, LCH, and VFA was carried out by the technique of hapten inhibition of precipitation reaction. The hapten inhibition assay results reveal that the presence of a methyl or methylene group at the O-2 or O-3 position of the sugar is essential for hydrophobic interaction with PSA, LCH, and VFA. The substitution of methyl by nitrobenzyl leads to enhanced binding (1.7-16.7 times for the 2-O-substituted compounds and 7.9-40.5 times for the 3-O-substituted compounds) with the m-nitrobenzyl group contributing to maximum binding. A hydrophobic interaction is also involved between Con A and 2-O-nitrobenzyl derivatives, resulting in enhanced binding, but the corresponding 3-O-isomers bind poorly due probably to steric reasons. These results may be rationalized on the basis of the recently published X-ray data of Con A and VFA. The nitrobenzyl derivatives, after transformation to their azido analogs, have potential applications in the photoaffinity labeling of these lectins. | en_US |
dc.format.extent | 780748 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Synthesis of high-affinity, hydrophobic monosaccharide derivatives and study of their interaction with concanavalin A, the pea, the lentil, and fava bean lectins | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.identifier.pmid | 1444465 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/29695/1/0000027.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(92)90274-Z | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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