In:
ChemBioChem, Wiley, Vol. 19, No. 14 ( 2018-07-16), p. 1507-1513
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.
Type of Medium:
Online Resource
ISSN:
1439-4227
,
1439-7633
DOI:
10.1002/cbic.201800087
Language:
English
Publisher:
Wiley
Publication Date:
2018
detail.hit.zdb_id:
2020469-3
SSG:
12
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