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Updated: Jan 30, 2026

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Development of Cell-type specific anti-HIV gp120 aptamers for siRNA delivery
Published on: June 23, 2011
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Modeling interaction between gp120 HIV protein and CCR5 receptor
I Guryanov1, F Real-Fernández2, G Sabatino2,3
1Institute of Chemistry, St. Petersburg State University, St. Petersburg, 198504, Russia.
Summary
Biomimetic nanotraps targeting HIV entry show promise. Nanoparticles with CCR5 receptor peptides and heparin effectively bind the HIV V3 loop, crucial for viral entry and potential therapeutic development.
Area of Science:
- Biomedical Engineering
- Virology
- Materials Science
Background:
- HIV entry into host cells is a critical target for diagnostics and therapeutics.
- Biomimetic nanodevices offer a novel approach to intercept viral particles.
- Previous work developed nanotraps targeting inflammatory chemokines via CCR5 receptor peptides.
Purpose of the Study:
- To investigate the interaction of biomimetic nanotraps with the V3 loop of the HIV gp120 protein.
- To evaluate the binding affinity of CCR5 receptor peptides (Nt and ECL2) to the V3 loop.
- To determine the role of heparin and CCR5 peptides in nanotraps for V3 loop binding.
Main Methods:
- Surface Plasmon Resonance (SPR) was used to measure binding kinetics and affinities.
- Synthesis and characterization of multilayer nanoparticles (nanotraps) with heparin and CCR5 peptides.
- Testing the binding of nanotraps and their peptide components to a V3 loop peptide.
Main Results:
- A conformational rearrangement occurs during V3 loop and CCR5 fragment binding.
- The ECL2 peptide exhibited higher affinity to the V3 peptide (KD = 3.72 × 10-8 M) than the Nt peptide (KD = 1.10 × 10-6 M).
- Heparin-coated nanotraps functionalized with CCR5 peptides demonstrated effective binding to the V3 loop, with both components being essential.
Conclusions:
- Short cationic peptides (ECL2 and Nt) derived from the CCR5 receptor are effective mimetics for V3 loop binding.
- The developed nanotraps show potential for targeting HIV-1 entry.
- Combined heparin and peptide functionalization is crucial for efficient V3 loop interaction.
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