Sequence‐Controlled Multi‐Block Glycopolymers to Inhibit DC‐SIGN‐gp120 Binding

Zhang, Qiang; Collins, Jennifer; Anastasaki, Athina; Wallis, Russell; Mitchell, Daniel A.; Becer, C. Remzi; Haddleton, David M.

doi:10.1002/ange.201300068

Cited by 67 publications

(52 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In particular, the fabrication of multivalent glycopolymer layers will foster the understanding of carbohydrate–protein (lectin) interactions and is crucial for selective and specific biomedical applications of lectin interactions with their glycan ligands, including novel‐biofunctionalized biomaterials for tissue engineering, and diagnostics and therapy …”

Section: Introductionmentioning

confidence: 99%

Glycopolymer Brushes for Specific Lectin Binding by Controlled Multivalent Presentation ofN-Acetyllactosamine Glycan Oligomers

Park

Rosencrantz

Elling

et al. 2014

Macromol. Rapid Commun.

View full text Add to dashboard Cite

A new multivalent glycopolymer platform for lectin recognition is introduced in this work by combining the controlled growth of glycopolymer brushes with highly specific glycosylation reactions. Glycopolymer brushes, synthetic polymers with pendant saccharides, are prepared by surface-initiated atom transfer radical polymerization (SI-ATRP) of 2-O-(N-acetyl-β-d-glucosamine)ethyl methacrylate (GlcNAcEMA). Here, the fabrication of multivalent glycopolymers consisting of poly(GlcNAcEMA) is reported with additional biocatalytic elongation of the glycans directly on the silicon substrate by specific glycosylation using recombinant glycosyltransferases. The bioactivity of the surface-grafted glycans is investigated by fluorescence-linked lectin assay. Due to the multivalency of glycan ligands, the glycopolymer brushes show very selective, specific, and strong interactions with lectins. The multiarrays of the glycopolymer brushes have a large potential as a screening device to define optimal-binding environments of specific lectins or as new simplified diagnostic tools for the detection of cancer-related lectins in blood serum.

show abstract

Section: Introductionmentioning

confidence: 99%

Glycopolymer Brushes for Specific Lectin Binding by Controlled Multivalent Presentation ofN-Acetyllactosamine Glycan Oligomers

Park

Rosencrantz

Elling

et al. 2014

Macromol. Rapid Commun.

View full text Add to dashboard Cite

show abstract

“…To render the synthetic glycopolymers as effective ligands for the practical targets, further precise design of the polymer structure; that is, the preparation of well‐defined multiblock glycocopolymers is a promising method. Haddleton and co‐workers prepared the sequence‐controlled glycopolymers by single‐electron transfer living radical polymerization (SET‐LRP) . However, the preparation of multiblock glycopolymers with the large number of block segments (> 5) by RAFT polymerization was not reported.…”

Section: Properties Of Aqueous Raft Polymerization For Preparation Ofmentioning

confidence: 99%

Quantitative preparation of multiblock glycopolymers bearing glycounits at the terminal segments by aqueous reversible addition–fragmentation chain transfer polymerization of acrylamide monomers

Nagao

Hoshino

Miura

2019

J. Polym. Sci. Part A: Polym. Chem.

View full text Add to dashboard Cite

Multiblock glycopolymers have gathered attention because of their potential use as effective ligands for sugar‐binding proteins. The authors report the quantitative preparation of multiblock glycopolymers by reversible addition‐fragmentation chain transfer polymerization. The optimized polymerization condition enabled the complete monomer incorporation into the elongating polymer chains at each polymerization step. The structure of the heptablock glycopolymer was well‐defined (polydispersity index <1.35), and their molecular recognition against lectins was evaluated.

show abstract

“…Although the most common application of SPR instruments is to determine affinity parameters for biomolecular interactions, 10 its versatility permits many other uses, including label-free immunoassays. [13][14][15] The novel assay described here involves several steps. Figure 1 summarizes the four steps required for studies with murine plasma (two mMBL isoforms); studies with rhMBL are limited to the first two steps.…”

Section: Spr-based Assaymentioning

confidence: 99%

A New Surface Plasmon Resonance Assay for In Vitro Screening of Mannose-Binding Lectin Inhibitors

et al. 2016

View full text Add to dashboard Cite

Mannose-binding lectin (MBL) is a circulating protein that acts as a soluble pattern recognition molecule of the innate immunity. It binds to carbohydrate patterns on the surface of pathogens or of altered self-cells, with activation of the lectin pathway of the complement system. Recent evidence indicates that MBL contributes to the pathophysiology of ischemiareperfusion injury and other conditions. Thus, MBL inhibitors offer promising therapeutic strategies, since they prevent the interaction of MBL with its target sugar arrays. We developed and characterized a novel assay based on surface plasmon resonance for in vitro screening of these compounds, which may be useful before the more expensive and time-consuming in vivo studies. The assay measures the inhibitor's ability to interfere with the binding of murine MBL-A or MBL-C, or of human recombinant MBL, to mannose residues immobilized on the sensor chip surface. We have applied the assay to measure the IC 50 of synthetic glycodendrimers, two of them with neuroprotective properties in animal models of MBLmediated injuries.

show abstract

Sequence‐Controlled Multi‐Block Glycopolymers to Inhibit DC‐SIGN‐gp120 Binding

Cited by 67 publications

References 40 publications

Glycopolymer Brushes for Specific Lectin Binding by Controlled Multivalent Presentation ofN-Acetyllactosamine Glycan Oligomers

Glycopolymer Brushes for Specific Lectin Binding by Controlled Multivalent Presentation ofN-Acetyllactosamine Glycan Oligomers

Quantitative preparation of multiblock glycopolymers bearing glycounits at the terminal segments by aqueous reversible addition–fragmentation chain transfer polymerization of acrylamide monomers

A New Surface Plasmon Resonance Assay for In Vitro Screening of Mannose-Binding Lectin Inhibitors

Contact Info

Product

Resources

About