Binding affinity and inhibitory potency of neomycin and streptomycin on the Tat peptide interaction with HIV-1 TAR RNA detected by on-line acoustic wave sensor.
The binding of two aminoglycoside antibiotics, neomycin and streptomycin, to a segment of the transactivation responsive region (TAR) RNA of the human immunodeficiency virus, and their inhibitory potency to disrupt the interaction of the RNA with a regulatory Tat protein-derived peptide, have been studied using a flow-through acoustic wave detector system. Binding affinity is directly correlated with the inhibitory potency of these molecules and the acoustic wave detection system shows that neomycin exhibits at least a ten-fold greater affinity for TAR RNA and that it is also a more potent inhibitor than streptomycin. These results are in agreement with previous studies. However, unlike the time-consuming batch-based assays, use of the flow-through format offers considerable potential for the rapid screening of the chemistry of relatively small-molecule-nucleic acid binding events.
Department of Chemistry, University of Toronto, 80 St. George St., Toronto, ON, Canada M5S 3H6.
Nardos
N
Tassew
Michael
M
Thompson
D000162:Acoustics; D000595:Amino Acid Sequence; D001360:Avidin / Q000494:pharmacology; D001483:Base Sequence; D004563:Electrochemistry; D015696:Gene Products, tat / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism; D016325:HIV Long Terminal Repeat / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009355:Neomycin / Q000494:pharmacology*; D012367:RNA, Viral / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013307:Streptomycin / Q000494:pharmacology*; D013997:Time Factors
D015696:Gene Products, tat; D012367:RNA, Viral; C093483:neutravidin; D001360:Avidin; D009355:Neomycin; D013307:Streptomycin