A Versatile Urea Type Linker for Functionalizing Natural Glycans and Its Validation in Glycan Arrays.

Autor: Serna S; Glycotechnology Group, Basque Research and Technology Alliance (BRTA) CIC biomaGUNE, Paseo Miramon 194, 20014, Donostia-San Sebastián, Spain., Artschwager R; Glycotechnology Group, Basque Research and Technology Alliance (BRTA) CIC biomaGUNE, Paseo Miramon 194, 20014, Donostia-San Sebastián, Spain.; Current address: Memorial Sloan Kettering Cancer Center New York, New York, 10065, USA., Pérez-Martínez D; Glycotechnology Group, Basque Research and Technology Alliance (BRTA) CIC biomaGUNE, Paseo Miramon 194, 20014, Donostia-San Sebastián, Spain., Lopez R; Organic Chemistry Department I, University of the Basque Country (UPV/EHU), Paseo Manuel Lardizabal 3, 20018, Donostia-San Sebastián, Spain., Reichardt NC; Glycotechnology Group, Basque Research and Technology Alliance (BRTA) CIC biomaGUNE, Paseo Miramon 194, 20014, Donostia-San Sebastián, Spain.; CIBER-BBN, Paseo Miramon 194, 20014, Donostia-San Sebastián, Spain.
Jazyk: angličtina
Zdroj: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2023 Sep 15; Vol. 29 (52), pp. e202301494. Date of Electronic Publication: 2023 Aug 10.
DOI: 10.1002/chem.202301494
Abstrakt: The isolation from organisms and readily available glycoproteins has become an increasingly convenient source of N-glycans for multiple applications including glycan microarrays, as reference standards in glycan analysis or as reagents that improve bioavailability of protein and peptide therapeutics through conjugation. A problematic step in the isolation process on a preparative scale can be the attachment of a linker for the improved purification, separation, immobilization and quantification of the glycan structures. Addressing this issue, we firstly aimed for the development of an UV active linker for a fast and reliable attachment to anomeric glycosylamines via urea bond formation. Secondly, we validated the new linker on glycan arrays in a comparative study with a collection of N-glycans which were screened against various lectins. In total, we coupled four structurally varied N-glycans to four different linkers, immobilized all constructs on a microarray and compared their binding affinities to four plant and fungal lectins of widely described specificity. Our study shows that the urea type linker showed an overall superior performance for lectin binding and once more, highlights the often neglected influence of the choice of linker on lectin recognition.
(© 2023 Wiley-VCH GmbH.)
Databáze: MEDLINE
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