Sequence-controlled multi-block glycopolymers to inhibit DC-SIGN-gp120 binding.
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چکیده
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منابع مشابه
Binding of “Clicked” Glycopolymers to SIGNR1 Synthetic Glycopolymers Show High Affinity Binding to SIGNR1, A Mouse Orthologue of Human DC-SIGN*
Background: Glycopolymers have previously been shown to bind to the C-type lectin DC-SIGN and inhibit interaction with HIV GP120. Results: SPR demonstrates that some glycopolymers exhibit strong binding to SIGNR1, an important murine homologue of DC-SIGN. Conclusion: Binding of certain polymers is comparable between SIGNR1 and DC-SIGN. Significance: Mouse lectins support glycopolymer binding, a...
متن کاملHigh-Affinity Glycopolymer Binding to Human DC-SIGN and Disruption of DC-SIGN Interactions with HIV Envelope Glycoprotein
Noncovalent interactions between complex carbohydrates and proteins drive many fundamental processes within biological systems, including human immunity. In this report we aimed to investigate the potential of mannose-containing glycopolymers to interact with human DC-SIGN and the ability of these glycopolymers to inhibit the interactions between DC-SIGN and the HIV envelope glycoprotein gp120....
متن کاملDendritic cell lectin-targeting sentinel-like unimolecular glycoconjugates to release an anti-HIV drug.
A series of cyclodextrin-based glycoconjugates, including glycoclusters and star glycopolymers, were synthesized via combination of CuAAC Huisgen coupling and copper-mediated living radical polymerization. These glycoconjugates showed high affinity binding to the human transmembrane lectin DC-SIGN and act as inhibitors to prevent the binding of HIV envelope protein gp120 to DC-SIGN at nanomolar...
متن کاملThe lectins griffithsin, cyanovirin-N and scytovirin inhibit HIV-1 binding to the DC-SIGN receptor and transfer to CD4(+) cells.
It is generally believed that during the sexual transmission of HIV-1, the glycan-specific DC-SIGN receptor binds the virus and mediates its transfer to CD4(+) cells. The lectins griffithsin (GRFT), cyanovirin-N (CV-N) and scytovirin (SVN) inhibit HIV-1 infection by binding to mannose-rich glycans on gp120. We measured the ability of these lectins to inhibit both the HIV-1 binding to DC-SIGN an...
متن کاملRole of the Carbohydrate-Binding Sites of Griffithsin in the Prevention of DC-SIGN-Mediated Capture and Transmission of HIV-1
BACKGROUND The glycan-targeting C-type DC-SIGN lectin receptor is implicated in the transmission of the human immunodeficiency virus (HIV) by binding the virus and transferring the captured HIV-1 to CD4(+) T lymphocytes. Carbohydrate binding agents (CBAs) have been reported to block HIV-1 infection. We have now investigated the potent mannose-specific anti-HIV CBA griffithsin (GRFT) on its abil...
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ورودعنوان ژورنال:
- Angewandte Chemie
دوره 52 16 شماره
صفحات -
تاریخ انتشار 2013