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Streptomycin (STR) an aminoglycoside antibiotic which is used against bacteria in human and animal infection, have serious side effects on different parts of human body. Therefore, there is a crucial need to detect trace amount of it in serum and food products. Aptamers are oligonucleotides or peptides, which bind their targets with high affinity and specificity. These properties make aptamers as suitable candidates for biosensing applications. A 79-mer ss-DNA aptamer was applied for the detection of small amount of STR in various aptasensors. But there is no structural information on the STR-binding aptamer and molecular details underlying the aptamer-STR binding remain unexplored. In this study we provided a 3D-structural model for 79-mer ss-DNA aptamer from the sequence. Using docking program and molecular dynamics (MD) simulation we predicted the binding pocket of ss-DNA aptamer. Our results show STR streptose ring is buried within the groove of DNA model and capped by non Watson-Crick bases. STR interacts with aptamer through forming stable hydrogen bonds. Our computational findings are in fair agreement with experimental results. With the atomic structural details, we gained new insight into the Apt-STR binding interaction that can help to further optimize aptamer efficiency in biosensing applications. Communicated by Ramaswamy H. Sarma

Three-dimensional modeling of streptomycin binding single-stranded DNA for aptamer-based biosensors, a molecular dynamics simulation approach