Exploring Rigid and Flexible Scaffolds to Develop Potent Glucuronic Acid Glycodendrimers for Dengue Virus Inhibition - PubMed
- ️Mon Jan 01 2024
Exploring Rigid and Flexible Scaffolds to Develop Potent Glucuronic Acid Glycodendrimers for Dengue Virus Inhibition
Alejandro Merchán et al. Bioconjug Chem. 2024.
Abstract
Multivalent glycodendrimers are valuable tools for studying carbohydrate-protein interactions, and their scaffolds represent important components to increase specificity and affinity. Previous work by our group described the preparation of a tetravalent glucuronic acid rigid dendron that binds with good affinity to the dengue virus envelope protein (KD = 22 μM). Herein, the chemical synthesis and binding analysis of three new sets of rigid, semirigid, and flexible glucuronic acid-based dendrimers bearing different levels of multivalency and their interactions with the dengue virus envelope protein are described. The different oligoalkynyl scaffolds were coupled to glucuronic acid azides by a copper-catalyzed azide-alkyne cycloaddition reaction through optimized synthetic strategies to afford the desired glycodendrimers with good yields. Surface plasmon resonance studies have demonstrated that glycodendrimers 12b and 12c, with flexible scaffolds, give the best binding interactions with the dengue virus envelope protein (12b: KD = 0.487 μM and 12c: KD = 0.624 μM). Their binding constant values were 45 and 35 times higher than the one obtained in previous studies with a rigid tetravalent glucuronic acid dendron (KD = 22 μM), respectively. Molecular modeling studies were carried out in order to understand the difference in behavior observed for 12b and 12c. This work reports an efficient glycodendrimer chemical synthesis process that provides an appropriate scaffold that offers an easy and versatile strategy to find new active compounds against the dengue virus.
Conflict of interest statement
The authors declare no competing financial interest.
Figures
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SPR measurement of GlcA GDs binding to immobilized DENV2 at 100 μM.
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Binding response of different concentrations of GDs 12b (A1) and 12c (B1) with DENV2 immobilized on the CM4 chip, showing association and dissociation phases. Responses were reference-subtracted and blank-corrected. Steady-state affinity study of the interaction between GDs 12b (A2) and 12c (B2) and DENV2 immobilized on a CM4 chip.
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Final MD pose of GDs 12b (A, C) and 12c (B, D) in DENV2. In (A) and (B) representation, the DENV2 protein is depicted as a white cartoon, lysine residues as pink sticks, and GDs as glue sticks. In (C) and (D) representation, GDs are shown as pink sticks and the protein is shown as an electrostatic surface calculated by APBS (negatively charged surface in red; positively charged surface in blue; hydrophobic surface in white). The difference in intensity of the colors is due to the position of the side chain residues on the surface after the simulation.
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Final poses of DENV2 bound to dendrimers 12b (A) and 12c (B). Protein is shown in cartoon mode gray with the relevant residues shown as green sticks. Dendrimers are represented as pink sticks, and the electrostatic interactions are represented as yellow dash lines.
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