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Sugar-decorated carbon dots: a novel tool for targeting immunomodulatory receptors.


ABSTRACT: Interactions between sialic acid (Sia) and sialic acid-binding immunoglobulin-like lectins (siglecs) regulate the immune system, with aberrations contributing to pathologies such as autoimmunity, infectious disease and cancer. Over the last decade, several multivalent Sia ligands have been synthesized to modulate the Sia-binding affinity of proteins/lectins. Here, we report a novel class of multivalent siglec probes through the decoration of α(2,6)-sialyllactose ligands on inherently fluorescent carbon dots (CD). We show that the preference of α(2,3)-linked Sia for siglec-1 can be altered by increasing the multivalence of Sia ligands present on the CD, and that a locally high glycan concentration can have a direct effect on linkage specificity. Additionally, micromolar (IC50 ∼ 70 μM) interaction of α(2,6)-sialyllactose-CD (6-CD) with siglec-2 (CD22) revealed it was capable of generating a significant cytotoxic effect on Burkitt's Lymphoma (BL) Daudi B cells. This phenonomen was attributed to 6-CD's ability to form trans interactions with CD22 on masked BL Daudi cells as a direct result of clustering of the Sia moiety on the CD surface. Overall, our glycoengineered carbon dots represent a novel high affinity molecular probe with multiple applications in sialoglycoscience and medicine.

SUBMITTER: Cooper O 

PROVIDER: S-EPMC9729803 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature

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Sugar-decorated carbon dots: a novel tool for targeting immunomodulatory receptors.

Cooper Oren O   Waespy Mario M   Chen Dechao D   Kelm Sørge S   Li Qin Q   Haselhorst Thomas T   Tiralongo Joe J  

Nanoscale advances 20221103 24


Interactions between sialic acid (Sia) and sialic acid-binding immunoglobulin-like lectins (siglecs) regulate the immune system, with aberrations contributing to pathologies such as autoimmunity, infectious disease and cancer. Over the last decade, several multivalent Sia ligands have been synthesized to modulate the Sia-binding affinity of proteins/lectins. Here, we report a novel class of multivalent siglec probes through the decoration of α(2,6)-sialyllactose ligands on inherently fluorescent  ...[more]

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