Diversity of C-linked neoglycopeptides for the exploration of subsite-assisted carbohydrate binding interactions

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DOIResolve DOI: http://doi.org/10.1016/S0960-894X(98)00182-6
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TypeArticle
Journal titleBioorganic & Medicinal Chemistry Letters
Volume8
Issue10
Pages11271132; # of pages: 6
AbstractDiversity of c~-galactose based C-linked neoglycopeptides (lb, 2b, 3c, 4d, and 5d) has been developed to explore the importance of subsite-assisted carbohydrate binding interactions. Deprotected C-linked neoglycopeptides (lb, 2b, 3c, 4d, and 5d) were synthesized and tested in competitive inhibition assays using a model enzyme-linked lectin (e.g., Maclura pomifera). Compound 2b, with two c~-galactoside units on the side chain of the lysine residue of the dipeptide backbone, exhibited a remarkable effect with a 2.82-fold increase in its inhibitory properties (IC50 1.48 raM) in comparison to lb (IC50 4.18 raM).
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Steacie Institute for Molecular Sciences
Peer reviewedNo
NPARC number12340914
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Record identifier105181df-f2e8-4754-98f9-895965cf885e
Record created2009-09-11
Record modified2016-05-09
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