Sunkari, Yashoda Krishna and Alam, Faiyaz and Kandiyal, Pancham Singh and Aloysius, Siriwardena and Ampapathi, Ravi Sankar and Chakraborty, Tushar Kanti (2016) Influence of Linker Length on Conformational Preferences of Glycosylated Sugar Amino Acid Foldamers. In: CHEMBIOCHEM, 17 (19). pp. 1839-1844.
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Abstract
Glycosylation of foldamers derived from furanoid sugar amino acids with mannose and a propyltriazole linker results in an unprecedented 16/10 mixed-turn structure in the glycopeptides in water, with a preference for the higher-order structure irrespective of the stereochemistry of the starting foldamer. This is in stark contrast to the structures displayed by the same oligomers in water when mannosylated with a two-carbon-shorter methyltriazole linker: 16-membered turn structure in the cis-foldamer and 10-membered in its trans congener. This demonstrates the defining influence of the linker length on the structural preference of these novel glycopeptide mimics.
Item Type: | Journal Article |
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Publication: | CHEMBIOCHEM |
Additional Information: | Copy right for this article belongs to the WILEY-V C H VERLAG GMBH, POSTFACH 101161, 69451 WEINHEIM, GERMANY |
Department/Centre: | Division of Chemical Sciences > Organic Chemistry |
Date Deposited: | 03 Dec 2016 06:50 |
Last Modified: | 03 Dec 2016 06:50 |
URI: | http://eprints.iisc.ac.in/id/eprint/55335 |
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