Journal
ANALYTICAL CHEMISTRY
Volume 88, Issue 4, Pages 2327-2334Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.5b04268
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Funding
- Regione Campania under POR Campania FESR [2007-2013-O.O. 2.1]
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By using a new rapid screening platform set on molecular docking simulations and fluorescence quenching techniques, three new anti-HIV aptamers targeting the viral surface glycoprotein 120 (gp120) were selected, synthesized, and assayed. The use of the short synthetic fluorescent peptide V35-Fluo mimicking the V3 loop of gp120, as the molecular target for fluorescence-quenching binding affinity studies, allowed one to measure the binding affinities of the new aptamers for the HIV-1 gp120 without the need to obtain and purify the full recombinant gp120 protein. The almost perfect correspondence between the calculated K-d and the experimental EC50 on NW-infected cells confirmed the reliability of the platform as an alternative to the existing methods for aptamer selection and measuring of aptamer-protein equilibria.
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