Sugar-modified Foldamers as Conformationally Defined and Biologically Distinct Glycopeptide Mimics
IR@CDRI: CSIR-Central Drug Research Institute, Lucknow
View Archive Info| Field | Value | |
| Creator |
Siriwardena, Aloysius
Pulukuri, K K Kandiyal, P S Roy, Saumya Bande, Omprakash Ghosh, Subhash Fernàndez, J M G Martin, F A Ghigo, Jean-Marc Beloin, Christophe Ito, Keigo Woods, R J Ampapathi, R S Chakraborty, T K |
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| Date |
2014-07-14T11:50:44Z
2014-07-14T11:50:44Z 2013 |
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| Identifier |
Angewandte Chemie International Edition, 2013, 52(39), 10221–10226
http://hdl.handle.net/123456789/1307 |
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| Description |
To fold or not to fold?: That the conformational preferences of foldamer backbones might be modulated by appended sugars and also that such effects might inform on the roles of glycans on the preferred secondary structures adopted by their natural glycopeptide counterparts, is the intriguing question posed. We demonstrate in this study that attached sugars do indeed play a defining role in the conformations adopted by a pair of novel SAA-derived foldamers in water and that these differences are reflected in the contrasting interactions of these glycofoldamers with various biological targets.
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| Format |
332670 bytes
application/pdf |
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| Language |
en
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| Relation |
CSIR-CDRI Communication No. 8490
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| Subject |
Sugar Amino acid (SAA)
Glycofoldamers Neoglycopeptides Solution conformational preferences Restrained molecular dynamics Protein-carbohydrate interactions |
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| Title |
Sugar-modified Foldamers as Conformationally Defined and Biologically Distinct Glycopeptide Mimics
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| Type |
Article
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