RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: 126
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAAAACGGUUCUGUGUGUGGACUAGCCGCGGCCGUUUUCGACAUGAGGCCCGGAUCCGGC3'
Sequence length: 80
GC content: 0.5875
Affinity: Kd1: 0.14 ±0.04 nM
Kd2: 11 ± 3 nM
Pool type: 5'-GGGAGCUCAGAAUAAACGCUCAA-30N-UUCGACAUGAGGCCCGGAUCCGGC-3'
Pool random region: 30
Binding buffer/conditions: Phosphate-buffered saline (PBS =10.1 mM Na2HP04, 1.8 mM KH2P04, 137 mM NaCl, and 2.7 mM KC1, pH 7.4)
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported 
Application as quoted in the referenced paper: Therapeutic: " We demonstrate that these ligands inhibit the initiating step of VEGF signaling:bindingof the growth factor to specific cell-surface receptors.This observation is relevant in view of the recent finding that basic fibroblast growth factor and VEGF have a strong synergistic effect on the induction of angiogenesis in vitro (Pepper etal., 1992). Oligonucleotide_x0002_based compounds, or their mimetic analogs, clearly have the potential for becoming a new class of potent and specific inhibitors of pathological angiogenesis. Efforts aimed toward the development of therapeutic as well as diagnostic agents based on our findings are in progress"
Additional information: Most RNA ligands exhibited biphasic binding to VEGF. For those ligands, binding of RNA to VEGF is described by a model in which the RN A is assumed to be partitioned between two noninterconverting components (Ri and R2) that bind to VEGF with different affinities. R1 is associated with kd1, and R2 is associated with kd2
Reference (1994, Biochemistry ): Jellinek, D., Green, L. S., Bell, C., & Janjić, N. (1994). Inhibition of receptor binding by high-affinity RNA ligands to vascular endothelial growth factor. Biochemistry, 33(34), 10450–10456. https://doi.org/10.1021/bi00200a028
Aptamer: DH25.42
Target: Adenosine and Adenosine Triphosphate (ATP)
Type of nucleic acid: ssDNA
Sequence: 5'CCTGGGGGAGTATTGCGGAGGAAGG3'
Sequence length: 25
GC content: 0.64
Affinity: Not reported
Pool type: 5'-AACACTATCCGACTGGCACC-N72-CCTTGGTCATTAGGATCC -3'
Pool random region: 72
Binding buffer/conditions: 300 mM NaCl, 5 mM MgCl2, 20 mM Tris, pH 7.6
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported 
Post-SELEX modifications: To see if the conserved and covarying sequences were sufficient for ATP binding, a 25 base oligonucleotide (DH25.42; Figure 5 A) that contained only these regions was synthesized. When this oligonucleotide was assayed for ATP binding, greater then 90% of the DNA remained on the ATP-agarose column after washing with 10 column vol_x0002_umes of buffer and was specifically eluted by ATP
Application as quoted in the referenced paper: Research: " The specificity of ATP binding exhibited by the DNA aptamer raises the possibility that some DNA sequences might be able to stabilize reaction transition states with respect to ground state structures and, thus, exhibit catalytic function. Furthermore, the RNA aptamer for ATP has been used as a starting point for the selection of ribozymes with polynucleotide kinase activity (Lorsch & Szostak, 1994b). Now that a DNA aptamer for ATP has been isolated, similar selections for catalytic DNAs can also be attempted"
Additional information: The pool of random-sequence RNA molecules that was used in this work has been previously described (Bartel & Szostak,1993).The mutagenized pool used in the secondary selection was based on the sequence 5'-GTGCTTGGGGGAGTATTGCGGAGGAAAGCGGCCCTGCTGAAG-3', flanked by the same primer binding sites as in the original random-sequence pool.
Reference (1995, Biochemistry ): Huizenga, D. E., & Szostak, J. W. (1995). A DNA aptamer that binds adenosine and ATP. Biochemistry, 34(2), 656–665. https://doi.org/10.1021/bi00002a033
Aptamer: clone 16
Target: Adenosine and Adenosine Triphosphate (ATP)
Type of nucleic acid: ssDNA
Sequence: 5'CTACCTGGGGGAGCATTGGGGAGGAAGGTAGCCGTGCGAAAA3'
Sequence length: 42
GC content: 0.5952380952380952
Affinity: Kd: 6 ± 3 uM
Pool type: 5'-AACACTATCCGACTGGCACC-N72-CCTTGGTCATTAGGATCC -3'
Pool random region: 72
Binding buffer/conditions: 300 mM NaCl, 5 mM MgCl2, 20 mM Tris, pH 7.6
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported 
Post-SELEX modifications: The binding domain of this aptamer was localized to a 42 base sequence by deletion analysis. (Truncation)
Application as quoted in the referenced paper: Research: " The specificity of ATP binding exhibited by the DNA aptamer raises the possibility that some DNA sequences might be able to stabilize reaction transition states with respect to ground state structures and, thus, exhibit catalytic function. Furthermore, the RNA aptamer for ATP has been used as a starting point for the selection of ribozymes with polynucleotide kinase activity (Lorsch & Szostak, 1994b). Now that a DNA aptamer for ATP has been isolated, similar selections for catalytic DNAs can also be attempted"
Additional information: The pool of random-sequence RNA molecules that was used in this work has been previously described (Bartel & Szostak,1993).The mutagenized pool used in the secondary selection was based on the sequence 5'-GTGCTTGGGGGAGTATTGCGGAGGAAAGCGGCCCTGCTGAAG-3', flanked by the same primer binding sites as in the original random-sequence pool.
Reference (1995, Biochemistry ): Huizenga, D. E., & Szostak, J. W. (1995). A DNA aptamer that binds adenosine and ATP. Biochemistry, 34(2), 656–665. https://doi.org/10.1021/bi00002a033
Aptamer: RT1
Target: Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
Type of nucleic acid: ssDNA
Sequence: 5'CCCCTGCAGGTGATTTTGCTCAAGTCAGAAGGATAAACTGTCCAGAACTTGGAATATATCAGTATCGCTAATCAGGCGGAT3'
Sequence length: 81
GC content: 0.4444444444444444
Affinity: Kd: 1 nM; Ki: <0.3 nM
Pool type: 5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
Pool random region: 35
Binding buffer/conditions: 200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Reference (1995, Biochemistry ): Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
Aptamer: RT1t49
Target: Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
Type of nucleic acid: ssDNA
Sequence: 5'CCCCTGCAGGTGATTTTGCTCAAGTCAGAAGGATAAACTGTCCAGAACTTGGA3'
Sequence length: 53
GC content: 0.4716981132075472
Affinity: Kd: 4 nM; 
Pool type: 5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
Pool random region: 35
Binding buffer/conditions: 200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Post-SELEX modifications: Truncated
Application as quoted in the referenced paper: Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Reference (1995, Biochemistry ): Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
Aptamer: RT4
Target: Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
Type of nucleic acid: ssDNA
Sequence: 5'CCCCTGCAGGTGATTTTGCTCAAGTTTAGCAAAGTTGAAGCCGGACTAACAAGCTCTACGAGTATCGCTAATCAGGCGGAT3'
Sequence length: 81
GC content: 0.4814814814814814
Affinity: Kd: 8 nM; Ki: 4 nM
Pool type: 5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
Pool random region: 35
Binding buffer/conditions: 200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Reference (1995, Biochemistry ): Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
Aptamer: RT6
Target: Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
Type of nucleic acid: ssDNA
Sequence: 5'CCCCTGCAGGTGATTTTGCTCAAGTCAGGCGTTAGGGAAGGGCGTCGAAAGCAGGGTGGGAGTATCGCTAATCAGGCGGAT3'
Sequence length: 81
GC content: 0.5679012345679012
Affinity: Kd: 5 nM; Ki: 30 nM
Pool type: 5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
Pool random region: 35
Binding buffer/conditions: 200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Reference (1995, Biochemistry ): Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
Aptamer: RT10
Target: Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
Type of nucleic acid: ssDNA
Sequence: 5'CCCCTGCAGGTGATTTTGCTCAAGTTATTTGCCCCTGCAGGCCGCAGGAGTGCTAGCAGTAGTATCGCTAATCAGGCGGAT3'
Sequence length: 81
GC content: 0.5432098765432098
Affinity: Kd: 11 nM;  Ki: 62 nM
Pool type: 5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
Pool random region: 35
Binding buffer/conditions: 200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Reference (1995, Biochemistry ): Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
Aptamer: RT12
Target: Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
Type of nucleic acid: ssDNA
Sequence: 5'CCCCTGCAGGTGATTTTGCTCAAGTCGATTAGGTCCCCTGCCGCTAAACAGCGCCGCGGTAAGTATCGCTAATCAGGCGGAT3'
Sequence length: 82
GC content: 0.5609756097560976
Affinity: Kd: 2 nM
Pool type: 5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
Pool random region: 35
Binding buffer/conditions: 200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Reference (1995, Biochemistry ): Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
Aptamer: RT36
Target: Reverse Transcriptase of Type 1 Human Immunodeficiency Virus (HIV-1 RT)
Type of nucleic acid: ssDNA
Sequence: 5'CCCCTGCAGGTGATTTTGCTCAAGTAAGCTCTTAGTTGATGCGCGGTCAAAATTTAAGCTAGTATCGCTAATCAGGCGGAT3'
Sequence length: 81
GC content: 0.4567901234567901
Affinity: Kd: 4 nM; Ki: 6.5 nM
Pool type: 5'-CCCCTGCAGGTGATTTTGCTCAAGT-N35-AGTATCGCTAATCAGGCGGAT-3'
Pool random region: 35
Binding buffer/conditions: 200 mM KOAc, 50 mM TrisHC1, pH 8.0, 6 mM MgCl2, and 10 mM DTT
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8
Molecular weight of target: 66 kDa (p66) polypeptide chain complexed with a 51 kDa (p51) polypeptide chain for a total weight of 117 kDa
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The importance of RT in the life cycle of HIV-1 and the lack of a natural function in the host cell make RT a preferred target for antiviral agents; high affinity and specificity for HIV-1 RT exhibited by the selected DNA ligands, along with their inhibitory effects, make them good candidates for structural investigations and potentially for therapeutic application"
Reference (1995, Biochemistry ): Schneider, D. J., Feigon, J., Hostomsky, Z., & Gold, L. (1995). High-affinity ssDNA inhibitors of the reverse transcriptase of type 1 human immunodeficiency virus. Biochemistry, 34(29), 9599–9610. https://doi.org/10.1021/bi00029a037
Aptamer: YT1
Target: Tax protein of the human T-cell lymphomatic virus (HTLV-1)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGCUUGGACUUAUUCUCGAGCCUGCAUGUGCUAGUCGACGUUGUUUCUGCAUCUUGAAAGAUGGGGCUGUGGGUGUGGUUACUUCUACGCGGUAUGCACUGUACGCCCCAUAUGUGCGUCUACAUGGAUCCUCA3'
Sequence length: 152
GC content: 0.5131578947368421
Affinity: Kd: 70 nM
Pool type: 5'-GGGAGAATTCCGACCAGAAGCTT-N120-CATATGTGCGTCTACATGGATCCTCA-3'
Pool random region: 120
Binding buffer/conditions: 20 mM Tris x Cl, pH 7.9, 80 mM KCl, 10% glycerol, 1 mM MgCl2, 0.2 mM EDTA, 10 microM DTT, 0.5 mM PMSF)
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.9
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " In order to develop reagents that could also be used to study protein:protein interactions, we have used in vitro selection to search for RNA aptamers that could interact with the transactivating protein Tax from human T-cell leukemia virus. The differential effects of our aptamer probe on protein:protein interactions suggest a model for how the transcription factor binding sites on the surface of the Tax protein are organized."
Additional information: DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection.

Reference (1995, RNA ): Tian, Y., Adya, N., Wagner, S., Giam, C. Z., Green, M. R., & Ellington, A. D. (1995). Dissecting protein:protein interactions between transcription factors with an RNA aptamer. RNA (New York, N.Y.), 1(3), 317–326.
Aptamer: X1
Target: Tobramycin
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGCUUCUGGUUAGUUUUGCACAGUGGUCGAUGCUAGACUUGGUUUAGGUAAUGAGUCCAAUAGUCCAUAUGUGCGUCUACAUGGAUCCUCA3'
Sequence length: 109
GC content: 0.4587155963302752
Affinity: Kd: 3 ± 1 nM (high affinity component); 15.9 ± 0.7 µM (low affinity component)
Pool type: 5'-GGGAGAAUUCCGACCAGAAGCUU-N60-CAUAUGUGCGUCUACAUGGAUCCUCA-3'
Pool random region: 60
Binding buffer/conditions: 140 mM NaCl, 5 mM KCl, 1 mM CaCl2, 1 mM MgCl2, and 20 mM Tris acetate at pH 7.4
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic, Detection, and Research: "When coupled with the use of high-resolution NMR and X-ray spectroscopic studies, it ought to be possible to define the specific ways in which RNA molecules recognize aminoglycoside antibiotics.This information will be important in the design of novel molecules that will bind to and interfere with the function of specific RNA structures. Molecules of this type could be useful as paradigms for the design of novel drugs."
Reference (1995, Chem Biol ): Wang, Y., & Rando, R. R. (1995). Specific binding of aminoglycoside antibiotics to RNA. Chemistry & biology, 2(5), 281–290. https://doi.org/10.1016/1074-5521(95)90047-0
Aptamer: J6
Target: Tobramycin
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAAGCUUAGUAUAGCGAGGUUUAGCUACACUCGUGCUGAUCGUUUGGUACGGGACCUGCGUGUAGCCCAUAUGUGCGUCUACAUGGAUCCUCA3'
Sequence length: 109
GC content: 0.5137614678899083
Affinity: Kd: 2 ± 1 nM (high affinity component); 6.0 ± 0.4 µM (low affinity component)
Pool type: 5'-GGGAGAAUUCCGACCAGAAGCUU-N60-CAUAUGUGCGUCUACAUGGAUCCUCA-3'
Pool random region: 60
Binding buffer/conditions: 140 mM NaCl, 5 mM KCl, 1 mM CaCl2, 1 mM MgCl2, and 20 mM Tris acetate at pH 7.4
Divalent salt: MgCl/CaCl
Buffer type: Tris Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic, Detection, and Research: "When coupled with the use of high-resolution NMR and X-ray spectroscopic studies, it ought to be possible to define the specific ways in which RNA molecules recognize aminoglycoside antibiotics.This information will be important in the design of novel molecules that will bind to and interfere with the function of specific RNA structures. Molecules of this type could be useful as paradigms for the design of novel drugs."
Reference (1995, Chem Biol ): Wang, Y., & Rando, R. R. (1995). Specific binding of aminoglycoside antibiotics to RNA. Chemistry & biology, 2(5), 281–290. https://doi.org/10.1016/1074-5521(95)90047-0
Aptamer: B
Target: Rous sarcoma virus (RSV)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAAUGCCUCGUGUCGAAGAAGGGUGGCGCGAGGGUAGGGUUUCGACAUGAGGCCCGGAUCCGGC3'
Sequence length: 84
GC content: 0.6071428571428571
Affinity: Kd: ~2-3 μg of viral protein per ml)
Pool type: 5'-GCCGGATCCGGGCCTCATGTCGAA-N40-TTGAGCGTTTATTCTGAGCTCCC-3'
Pool random region: 40
Binding buffer/conditions: 2.5 mM MgCl2/100 mM NaCl/20 mM Tris HCl, pH 7.5
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The selection of the anti-RSV RNA and RNA analogs by intact virions immediately suggests the potential application of this approach to develop RNA and RNA analogs as inhibitors of other viruses such as human immunodeficiency virus. Aptamers change the structures of viral surface proteins so that these proteins can no longer function in steps critical for viral infection, such as viral attachment and virus-cell membrane fusion. Alternatively, some of the structural changes may trigger pathways to inhibit the steps which normally occur after virus internalization, such as the uncoating and the expression of the virus genome."
Additional information: 2'F-RNA: 2'-F-CTP and 2'-F-UTP replaced CTP and UTP. Transcribed a pool of 2'-F-RNA from unmodified RNA after 9 cycles of selection by RSV
Reference (1995, Proc Natl Acad Sci U S A ): Pan, W., Craven, R. C., Qiu, Q., Wilson, C. B., Wills, J. W., Golovine, S., & Wang, J. F. (1995). Isolation of virus-neutralizing RNAs from a large pool of random sequences. Proceedings of the National Academy of Sciences of the United States of America, 92(25), 11509–11513. https://doi.org/10.1073/pnas.92.25.11509
Aptamer: E
Target: Rous sarcoma virus (RSV)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAAUGUAGUGAACAUUAAUGGAGAGAGGGAGGGUAGGGUUACGUUCGACAUGAGGCCCGGAUCCGGC3'
Sequence length: 87
GC content: 0.5287356321839081
Affinity: Not reported
Pool type: 5'-GCCGGATCCGGGCCTCATGTCGAA-N40-TTGAGCGTTTATTCTGAGCTCCC-3'
Pool random region: 40
Binding buffer/conditions: 2.5 mM MgCl2/100 mM NaCl/20 mM Tris HCl, pH 7.5
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The selection of the anti-RSV RNA and RNA analogs by intact virions immediately suggests the potential application of this approach to develop RNA and RNA analogs as inhibitors of other viruses such as human immunodeficiency virus. Aptamers change the structures of viral surface proteins so that these proteins can no longer function in steps critical for viral infection, such as viral attachment and virus-cell membrane fusion. Alternatively, some of the structural changes may trigger pathways to inhibit the steps which normally occur after virus internalization, such as the uncoating and the expression of the virus genome."
Additional information: 2'F-RNA: 2'-F-CTP and 2'-F-UTP replaced CTP and UTP. Transcribed a pool of 2'-F-RNA from unmodified RNA after 9 cycles of selection by RSV
Reference (1995, Proc Natl Acad Sci U S A ): Pan, W., Craven, R. C., Qiu, Q., Wilson, C. B., Wills, J. W., Golovine, S., & Wang, J. F. (1995). Isolation of virus-neutralizing RNAs from a large pool of random sequences. Proceedings of the National Academy of Sciences of the United States of America, 92(25), 11509–11513. https://doi.org/10.1073/pnas.92.25.11509