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Conformation Analysis of GalNAc‐Appended Sugar Amino Acid Foldamers as Glycopeptide Mimics
Author(s) -
Sunkari Yashoda Krishna,
Pulukuri Kiran Kumar,
Kandiyal Pancham Singh,
Vaishnav Jayanti,
Ampapathi Ravi Sankar,
Chakraborty Tushar Kanti
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800087
Subject(s) - foldamer , glycopeptide , chemistry , glycoconjugate , stereochemistry , hydrogen bond , sequence (biology) , amino acid , biochemistry , molecule , organic chemistry , antibiotics
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.