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Characterization of New DNA Aptamers for Anti‐HIV‐1 Reverse Transcriptase
Author(s) -
Ratanabunyong Siriluk,
Aeksiri Niran,
Yanaka Saeko,
YagiUtsumi Maho,
Kato Koichi,
Choowongkomon Kiattawee,
Hangbua Supa
Publication year - 2021
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000633
Subject(s) - reverse transcriptase , aptamer , dna , dna polymerase , polymerase , nucleoside , mutant , chemistry , microbiology and biotechnology , nucleoside reverse transcriptase inhibitor , enzyme , biology , virology , biochemistry , polymerase chain reaction , gene
HIV‐1 RT is a necessary enzyme for retroviral replication, which is the main target for antiviral therapy against AIDS. Effective anti‐HIV‐1 RT drugs are divided into two groups; nucleoside inhibitors (NRTI) and non‐nucleoside inhibitors (NNRTI), which inhibit DNA polymerase. In this study, new DNA aptamers were isolated as anti‐HIV‐1 RT inhibitors. The selected DNA aptamer (WT62) presented with high affinity and inhibition against wild‐type (WT) HIV‐1 RT and gave a KD value of 75.10±0.29 nM and an IC 50 value of 84.81±8.54 nM. Moreover, WT62 decreased the DNA polymerase function of K103 N/Y181 C double mutant (KY) HIV‐1 RT by around 80 %. Furthermore, the ITC results showed that this aptamer has small binding enthalpies with both WT and KY HIV‐1 RTs through which the complex might form a hydrophobic interaction or noncovalent bonding. The NMR result also suggested that the WT62 aptamer could bind with both WT and KY mutant HIV‐1 RTs at the connection domain.