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Updated: Feb 11, 2026

Glycopeptide Capture for Cell Surface Proteomics
Published on: May 9, 2014
Conformation Analysis of GalNAc-Appended Sugar Amino Acid Foldamers as Glycopeptide Mimics
Yashoda Krishna Sunkari1, Kiran Kumar Pulukuri1, Pancham Singh Kandiyal1
1Centre for Nuclear Magnetic Resonance, SAIF, CSIR-Central Drug Research Institute, Lucknow, 226031, India.
Abstract:
Sugar amino acid (SAA)-based foldamers with well-defined secondary structures were appended with N-acetylgalactosamine (GalNAc) sugars to access sequence-defined, multidentate glycoconjugates with full control over number, spacing and position. Conformation analysis of these glycopeptides by extensive NMR spectroscopic studies revealed that the appended GalNAc units had a profound influence on the native conformational behaviour of the SAA foldamers. Whereas the 2,5-cis glycoconjugate showed a helical structure in water, comprising of two consecutive 16-membered hydrogen bonds, its 2,5-trans congener displayed an unprecedented 16/10-mixed turn structure not seen before in any glycopeptide foldamer.
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