Počet záznamů: 1
Glycan-decorated HPMA copolymers as high-affinity lectin ligands
- 1.0474869 - MBÚ 2018 RIV GB eng J - Článek v odborném periodiku
Bojarová, Pavla - Chytil, Petr - Mikulová, Barbora - Bumba, Ladislav - Konefal, Rafal - Pelantová, Helena - Krejzová, Jana - Slámová, Kristýna - Petrásková, Lucie - Kotrchová, Lenka - Cvačka, Josef - Etrych, Tomáš - Křen, Vladimír
Glycan-decorated HPMA copolymers as high-affinity lectin ligands.
Polymer Chemistry. Roč. 8, č. 17 (2017), s. 2647-2658. ISSN 1759-9954. E-ISSN 1759-9962
Grant CEP: GA ČR GC15-02578J; GA MZd(CZ) NV16-28594A; GA MŠMT(CZ) LD15085; GA MŠMT(CZ) LM2015064; GA MŠMT(CZ) LO1507
Institucionální podpora: RVO:61388971 ; RVO:61389013 ; RVO:61388963
Klíčová slova: BETA-N-ACETYLHEXOSAMINIDASE * WHEAT-GERM-AGGLUTININ * CLICK CHEMISTRY
Obor OECD: Biochemistry and molecular biology; Polymer science (UMCH-V); Polymer science (UOCHB-X)
Impakt faktor: 4.927, rok: 2017
Novel conjugates of N-(2- hydroxypropyl) methacrylamide (HPMA) copolymers tethered with chitooligosaccharidic epitopes of varying lengths were shown to be potent ligands of a model lectin, wheat germ agglutinin (WGA). The azide-functionalized oligosaccharidic epitopes were prepared by the action of Tyr470Asn mutant alpha-N-acetylhexosaminidase from Talaromyces flavus in a single reaction step and were conjugated to HPMA copolymer precursors in a defined pattern and density through Cu+- catalyzedazide-alkyne cycloaddition. The soluble, biocompatible, and structurally flexible synthetic glycopolymers were studied for their binding to WGA in a competitive enzyme-linked lectin assay (ELLA), and the kinetics of interaction were analyzed by surface plasmon resonance (SPR). To the best of our knowledge, this study presents the first HPMA copolymers derivatized with long oligosaccharides that demonstrate high affinity to a lectin target. The binding affinities in the low nanomolar and subnanomolar ranges place the prepared glycopolymers among the best WGA ligands reported to date. This study demonstrates the targeting potential of these glycopolymers for therapeutically relevant lectins.
Trvalý link: http://hdl.handle.net/11104/0271798
Počet záznamů: 1