RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: F
Target: Rous sarcoma virus (RSV)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAAAUUGUCUUGAACCCGUGGGAGGUGUGAGGGUAGGGGUGGUUCGACAUGAGGCCCGGAUCCGGC3'
Sequence length: 86
GC content: 0.5813953488372093
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
Aptamer: NX-213
Target: Vascular pemeability factor/vascular endothelial growth factor (VPF/VEGF)
Type of nucleic acid: 2'-amino-RNA
Sequence: 5'ACCCUGAUGGUAGACGCCGGGGUG3'
Sequence length: 24
GC content: 0.6666666666666666
Affinity: Kd: 2.4 ± 0.5 nM
Pool type: 5'-GGGAGACAAGAAUAACGCUCAA-N30-UUCGACAGGAGGCUCACAACAGGC-3'
Pool random region: 30
Binding buffer/conditions: PBS: 10.1 mM Na2HP04, 1.8 mM KH2PO4, 137 mM NaCl and 2.7 mM KCl, pH 7.4
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: NX-213 is a minimal ligand derived from aptamer 24a (Truncated). [5'P] represents the 5' cap, d(tstststs), where s represents the internucleoside phosphorothioate linkage, and [3'p] represents the 3' cap, d(tstststst); all pyrimidines are aminopyrimidines; positions 1, 9, 12, 13, 16, 19-22, 24 are 2'-ome purines

Of the 14 ribopurines in this minimal ligand, 10 can be substituted with the corresponding 2'-0-methylpurine nucleotides without a reduction in binding affinity toVPF/VEGF. In fact, the 2'- O-methyl substitution at permissive positions leads to a -17-fold improvement in the binding affinity to VPF/VEGEThe higher affinity results from the reduction in the dissociation rate constant of the 2'-O-methyl-sub_x0002_stituted RNA ligand from the protein compared to the unsubstituted ligand. The 2'-O-methyl-substituted minimal ligand, which folds into a bulged hairpin motif, is also more thermally stable than the unsubstituted ligand. Nuclease resistance of the ligand is further improved by the 2'-O-methyl substitutions and the addition of short phosphorothioate caps to the 3'- and 5'-ends.
Application as quoted in the referenced paper: Therapeutic: " The ability to produce and secrete VPF/VEGF is shared by many, if not most, tumor cells [5-7,10,18-22].There is now considerable evidence that VPF/VEGF secreted by tumors acts in a paracrine manner on the adjacent endothelial cells [23,24]; Since disregulated proliferation of blood vessels contributes to the pathology of many other disease states including psoriasis, rheumatoid arthritis and retinopathies [2] in whichVPF/VEGF may be important, there is a substantial impetus for the discovery of specific and potent ligandsiantagonists ofVPF/VEGF."
Additional information: 2′-amino-2′-deoxypyrimidine nucleotide RNA modifeid library
Reference (1995, Chem Biol ): Green, L. S., Jellinek, D., Bell, C., Beebe, L. A., Feistner, B. D., Gill, S. C., Jucker, F. M., & Janjić, N. (1995). Nuclease-resistant nucleic acid ligands to vascular permeability factor/vascular endothelial growth factor. Chemistry & biology, 2(10), 683–695. https://doi.org/10.1016/1074-5521(95)90032-2
Aptamer: NX-178
Target: Vascular pemeability factor/vascular endothelial growth factor (VPF/VEGF)
Type of nucleic acid: 2'-amino-RNA
Sequence: 5'ACCCUGAUGGUAGACGCCGGGGUG3'
Sequence length: 24
GC content: 0.6666666666666666
Affinity: Kd: 0.14 ± 0.01 nM
Pool type: 5'-GGGAGACAAGAAUAACGCUCAA-N30-UUCGACAGGAGGCUCACAACAGGC-3'
Pool random region: 30
Binding buffer/conditions: PBS: 10.1 mM Na2HP04, 1.8 mM KH2PO4, 137 mM NaCl and 2.7 mM KCl, pH 7.4
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: NX-178 is a minimal ligand derived from aptamer 24a. [5'P] represents the 5' cap, d(tstststs), where s represents the internucleoside phosphorothioate linkage, and [3'p] represents the 3' cap, d(tstststst); all pyrimidines are aminopyrimidines; NO 2'- O-methyl substitution
Application as quoted in the referenced paper: Therapeutic: " The ability to produce and secrete VPF/VEGF is shared by many, if not most, tumor cells [5-7,10,18-22].There is now considerable evidence that VPF/VEGF secreted by tumors acts in a paracrine manner on the adjacent endothelial cells [23,24]; Since disregulated proliferation of blood vessels contributes to the pathology of many other disease states including psoriasis, rheumatoid arthritis and retinopathies [2] in whichVPF/VEGF may be important, there is a substantial impetus for the discovery of specific and potent ligandsiantagonists ofVPF/VEGF."
Additional information: 2′-amino-2′-deoxypyrimidine nucleotide RNA modifeid library
Reference (1995, Chem Biol ): Green, L. S., Jellinek, D., Bell, C., Beebe, L. A., Feistner, B. D., Gill, S. C., Jucker, F. M., & Janjić, N. (1995). Nuclease-resistant nucleic acid ligands to vascular permeability factor/vascular endothelial growth factor. Chemistry & biology, 2(10), 683–695. https://doi.org/10.1016/1074-5521(95)90032-2
Aptamer: 24A
Target: Vascular pemeability factor/vascular endothelial growth factor (VPF/VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGACAAGAAUAACGCUCAAACCCUGAUGGUAGACGCCGGGGUGCCGGAAUUCGACAGGAGGCUCACAACAGGC3'
Sequence length: 76
GC content: 0.5789473684210527
Affinity: Not reported
Pool type: 5'-GGGAGACAAGAAUAACGCUCAA-N30-UUCGACAGGAGGCUCACAACAGGC-3'
Pool random region: 30
Binding buffer/conditions: PBS: 10.1 mM Na2HP04, 1.8 mM KH2PO4, 137 mM NaCl and 2.7 mM KCl, pH 7.4
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " The ability to produce and secrete VPF/VEGF is shared by many, if not most, tumor cells [5-7,10,18-22].There is now considerable evidence that VPF/VEGF secreted by tumors acts in a paracrine manner on the adjacent endothelial cells [23,24]; Since disregulated proliferation of blood vessels contributes to the pathology of many other disease states including psoriasis, rheumatoid arthritis and retinopathies [2] in whichVPF/VEGF may be important, there is a substantial impetus for the discovery of specific and potent ligandsiantagonists ofVPF/VEGF."
Reference (1995, Chem Biol ): Green, L. S., Jellinek, D., Bell, C., Beebe, L. A., Feistner, B. D., Gill, S. C., Jucker, F. M., & Janjić, N. (1995). Nuclease-resistant nucleic acid ligands to vascular permeability factor/vascular endothelial growth factor. Chemistry & biology, 2(10), 683–695. https://doi.org/10.1016/1074-5521(95)90032-2
Aptamer: P5
Target: Human immunodeficiency virus (HIV-1) integrase
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAACCAGUCUUGUGGCUUUGAAAGAGAGGAGUGUUCGACAUGAGGCCCGGAUCCGGC3'
Sequence length: 77
GC content: 0.5454545454545454
Affinity: Kd: 12 nM in a buffer containing 250 mM NaCl; 2 nM in a buffer contining 50 mM NaCl
Pool type: 5'-GGGAGCUCAGAAUAAACGCUCAA-N30-UUCGACAUGAGGCCCGGAUCCGGC-3'
Pool random region: 30
Binding buffer/conditions: 10 mM Tris-HCl pH 8.4, 50 mM KCl, 7.5 mM MgCl2, 0.05 mg/ml BSA
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 8.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " Integrase associates with double-stranded HIV DNA to form a preintegration complex which is transported into the nucleus of infected cells; Because integrase is essential for a productive infection, we felt that it would serve as a reasonable target for antiviral therapeutics"
Reference (1995, Virology ): Allen, P., Worland, S., & Gold, L. (1995). Isolation of high-affinity RNA ligands to HIV-1 integrase from a random pool. Virology, 209(2), 327–336. https://doi.org/10.1006/viro.1995.1264
Aptamer: PS2
Target: N-methylmesoporphyrin IX (NMM)
Type of nucleic acid: ssDNA
Sequence: 5'TTGCCTAACCGTGAAGGTAAAACGATTTAGTCAAAGTGGGAGGGCGGTGGTGTTGACTGATCGATTTTATTCCA3'
Sequence length: 74
GC content: 0.4459459459459459
Affinity: Kd: 0.5 µM
Pool type: 5‘-GGATCTTTTTGATCCGGTCGGCACC-N76-CCTTGG-N76-GGCACC-N76-CCTTGGGTCATTAGGCGA-3'
Pool random region: 76
Binding buffer/conditions: 0.1 M phosphate buffer (pH 4.0)
Buffer type: PBS/phosphate buffers
pH: 4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " Ultraviolet-visible absorption and circular dichroism spectroscopy of the DNA-NMM complexes indicates, however, that the interaction is not primarily intercalative in nature. The preferential binding of NMM by these aptamers raises the possibility of their being able to catalyze the chelation of metal ions by the porphyrin MPIX."
Additional information: DNA Library. The random-sequence DNA library used in this work was constructed according to the method of Bartel and Szostak (1993), with minor modifications. Two synthetic polynucleotides, R1 (5‘-TTGATCCGGTCGGCACC-N76- CCTTGGGTCATTAGGCGA) and, R2 (5‘-CGGGACTCTGACCTTGG-N76- GGCACCTGTCCACGCTC), were each rendered double-stranded by PCR. R1 was divided into two pools and restriction-digested, one pool with BanI (cutting at GGCACC) and the other with StyI (cutting at CCTTGG); R2 was digested with both enzymes. A 2-fold ligation was then carried out with T4 DNA ligase, to give duplexes of the form R1−R2−R1, containing a total of 228 random base pairs (bp). Ligated product (540 μg) was obtained, corresponding to 1.8 × 1015 different molecules. This library was then amplified with a large-scale (500 mL) PCR, using the primers R1P1−biotin (5‘-biotin-TCGCCTAATGACCCAAGG) and RLS (5‘-GGATCTTTTTGATCCGGTCGGCACC).
Reference (1996, Biochemistry ): Li, Y., Geyer, C. R., & Sen, D. (1996). Recognition of anionic porphyrins by DNA aptamers. Biochemistry, 35(21), 6911–6922. https://doi.org/10.1021/bi960038h
Aptamer: SLB10-1
Target: Aminoglycoside lividomycin
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAUGGAUCCACAUCUACGAAUUCAACGAGUGCAGUGGGAAACAGGUCUUUGGCUUCACUGCAGACUUGACGAAGCUU3'
Sequence length: 80
GC content: 0.4875
Affinity: Not reported
Pool type: 5'-GGGAAUGGAUCCACAUCUACGAAUUC-N30-UUCACUGCAGACUUGACGAAGCUU-3'
Pool random region: 30
Binding buffer/conditions: 500 mM NaC1, 50 mM Tris.HC1, pH 7.6)
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic " and Drug Development: Method turns the drug-discovery paradigm of engineering compounds for targets on its head, and instead seeks targets for the myriad new leads that are produced by combinatorial chemistry. Our results suggest that this new method for screening chemical libraries should work in practice, and show that such screens can yield interesting and medically relevant leads for nucleicacid-binding drugs"
Reference (1996, Mol Divers ): Lato, S. M., & Ellington, A. D. (1996). Screening chemical libraries for nucleic-acid-binding drugs by in vitro selection: a test case with lividomycin. Molecular diversity, 2(1-2), 103–110. https://doi.org/10.1007/BF01718707
Aptamer: SLB10-34
Target: Aminoglycoside lividomycin
Type of nucleic acid: ssRNA
Sequence: 5'GGGAAUGGAUCCACAUCUACGAAUUCCCGUCAAGUCCGGUAAGGUGCCUGACGUCUUCACUGCAGACUUGACGAAGCUU3'
Sequence length: 79
GC content: 0.5189873417721519
Affinity: Not reported
Pool type: 5'-GGGAAUGGAUCCACAUCUACGAAUUC-N30-UUCACUGCAGACUUGACGAAGCUU-3'
Pool random region: 30
Binding buffer/conditions: 500 mM NaC1, 50 mM Tris.HC1, pH 7.6)
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic " and Drug Development: Method turns the drug-discovery paradigm of engineering compounds for targets on its head, and instead seeks targets for the myriad new leads that are produced by combinatorial chemistry. Our results suggest that this new method for screening chemical libraries should work in practice, and show that such screens can yield interesting and medically relevant leads for nucleicacid-binding drugs"
Reference (1996, Mol Divers ): Lato, S. M., & Ellington, A. D. (1996). Screening chemical libraries for nucleic-acid-binding drugs by in vitro selection: a test case with lividomycin. Molecular diversity, 2(1-2), 103–110. https://doi.org/10.1007/BF01718707
Aptamer: ag.06
Target: L-arginine
Type of nucleic acid: ssRNA
Sequence: 5'GGAGCUCAGCCUUCACUGCAUGAUAAACCGAUGCUGGGCGAUUCUCCUGAAGUAGGGGAAGAGUUGUCAUGUAUGGGGGCACCACGGUCGGAUCCUG3'
Sequence length: 97
GC content: 0.5567010309278351
Affinity: Kd: 330 nM
Pool type: 5'GGAGCUCAGCCUUCACUGC-N74-GGCACCACGGUCGGAUCC-3'
Pool random region: 74
Binding buffer/conditions: 250 mM NaCl, 50 mM Tris–HCl pH 7.6, 5 mM MgCl2
Divalent salt: MgCl
Buffer type: Tris Buffers
pH: 7.6
Molecular weight of target: Not reported
Post-SELEX modifications: A chemical modification analysis with DMS, kethoxal and CMCT in the presence and absence of L-arginine in order to examine the secondary structure
Application as quoted in the referenced paper: Detection: " The interactions in the full length HIV-1 Tat–protein–TAR complex cannot be mimicked by arginine alone, but high resolution NMR analyses have allowed to relate structural differences observed in the free TAR–RNA and the Tat–TAR complex to individual arginine residues. Analogously, the identification and characterization of DNA or RNA motifs such as the one described here will help to give new insights into the principles of RNA–protein and RNA–ligand interactions."
Reference (1996, Nucleic Acids Res ): Geiger, A., Burgstaller, P., von der Eltz, H., Roeder, A., & Famulok, M. (1996). RNA aptamers that bind L-arginine with sub-micromolar dissociation constants and high enantioselectivity. Nucleic acids research, 24(6), 1029–1036. https://doi.org/10.1093/nar/24.6.1029
Aptamer: 36t
Target: Platelet-derived growth factor (PDGF)-AB
Type of nucleic acid: ssDNA
Sequence: 5'CACAGGCTACGGCACGTAGAGCATCACCATGATCCTGTG3'
Sequence length: 40
GC content: 0.55
Affinity: Kd: 0.094 ± 0.011 nM
Pool type: 5‘-CCGAAGCTTAATACGACTCACTATAGGGATCCGCCTGATTAGCGATACT-N40-ACTTGAGCAAAATCACCTGCAGGGG-3‘
Pool random region: 40
Binding buffer/conditions: PBSM (10.1 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl and 2.7 mM KCl, 1 mM MgCl2, pH 7.4) containing 0.01% human serum albumin (HSA)
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Deduced from the knowledge of the consensus motif
Application as quoted in the referenced paper: Therapeutic: " Many tumor cell lines have since been shown to produce and secrete PDGF, some of which also express the cognate PDGF receptors; paracrine effect on the tumor stroma and, in some tumor cell lines, autocrine growth stimulation by PDGF are therefore possible; These DNA ligands therefore represent lead compounds for a novel class of high-affinity, specific antagonists of PDGF-AB and PDGF-BB."
Additional information: [3′T] represents a 3′-3′-linked thymidine nucleotide added to reduce 3′-exonuclease-mediated degradation
Reference (1996, Biochemistry ): Green, L. S., Jellinek, D., Jenison, R., Ostman, A., Heldin, C. H., & Janjic, N. (1996). Inhibitory DNA ligands to platelet-derived growth factor B-chain. Biochemistry, 35(45), 14413–14424. https://doi.org/10.1021/bi961544+
Aptamer: 36t
Target: Platelet-derived growth factor (PDGF)-AA
Type of nucleic acid: ssDNA
Sequence: 5'CACAGGCTACGGCACGTAGAGCATCACCATGATCCTGTG3'
Sequence length: 40
GC content: 0.55
Affinity: Kd: 72 ± 12 nM
Pool type: 5‘-CCGAAGCTTAATACGACTCACTATAGGGATCCGCCTGATTAGCGATACT-N40-ACTTGAGCAAAATCACCTGCAGGGG-3‘
Pool random region: 40
Binding buffer/conditions: PBSM (10.1 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl and 2.7 mM KCl, 1 mM MgCl2, pH 7.4) containing 0.01% human serum albumin (HSA)
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Deduced from the knowledge of the consensus motif
Application as quoted in the referenced paper: Therapeutic: " Many tumor cell lines have since been shown to produce and secrete PDGF, some of which also express the cognate PDGF receptors; paracrine effect on the tumor stroma and, in some tumor cell lines, autocrine growth stimulation by PDGF are therefore possible; These DNA ligands therefore represent lead compounds for a novel class of high-affinity, specific antagonists of PDGF-AB and PDGF-BB."
Additional information: [3′T] represents a 3′-3′-linked thymidine nucleotide added to reduce 3′-exonuclease-mediated degradation
Reference (1996, Biochemistry ): Green, L. S., Jellinek, D., Jenison, R., Ostman, A., Heldin, C. H., & Janjic, N. (1996). Inhibitory DNA ligands to platelet-derived growth factor B-chain. Biochemistry, 35(45), 14413–14424. https://doi.org/10.1021/bi961544+
Aptamer: 36t
Target: Platelet-derived growth factor (PDGF)-BB
Type of nucleic acid: ssDNA
Sequence: 5'CACAGGCTACGGCACGTAGAGCATCACCATGATCCTGTG3'
Sequence length: 40
GC content: 0.55
Affinity: Kd: 0.093± 0.009 nM
Pool type: 5‘-CCGAAGCTTAATACGACTCACTATAGGGATCCGCCTGATTAGCGATACT-N40-ACTTGAGCAAAATCACCTGCAGGGG-3‘
Pool random region: 40
Binding buffer/conditions: PBSM (10.1 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl and 2.7 mM KCl, 1 mM MgCl2, pH 7.4) containing 0.01% human serum albumin (HSA)
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Deduced from the knowledge of the consensus motif
Application as quoted in the referenced paper: Therapeutic: " Many tumor cell lines have since been shown to produce and secrete PDGF, some of which also express the cognate PDGF receptors; paracrine effect on the tumor stroma and, in some tumor cell lines, autocrine growth stimulation by PDGF are therefore possible; These DNA ligands therefore represent lead compounds for a novel class of high-affinity, specific antagonists of PDGF-AB and PDGF-BB."
Additional information: [3′T] represents a 3′-3′-linked thymidine nucleotide added to reduce 3′-exonuclease-mediated degradation
Reference (1996, Biochemistry ): Green, L. S., Jellinek, D., Jenison, R., Ostman, A., Heldin, C. H., & Janjic, N. (1996). Inhibitory DNA ligands to platelet-derived growth factor B-chain. Biochemistry, 35(45), 14413–14424. https://doi.org/10.1021/bi961544+
Aptamer: 41
Target: Platelet-derived growth factor (PDGF)-AB
Type of nucleic acid: ssDNA
Sequence: 5'CCGAAGCTTAATACGACTCACTATAGGGATCCGCCTGATTAGCGATACTTACTCAGGGCACTGCAAGCAATTGTGGTCCCAATGGGCTGAGTAACTTGAGCAAAATCACCTGCAGGGG3'
Sequence length: 118
GC content: 0.5
Affinity: Not reported
Pool type: 5‘-CCGAAGCTTAATACGACTCACTATAGGGATCCGCCTGATTAGCGATACT-N40-ACTTGAGCAAAATCACCTGCAGGGG-3‘
Pool random region: 40
Binding buffer/conditions: PBSM (10.1 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl and 2.7 mM KCl, 1 mM MgCl2, pH 7.4) containing 0.01% human serum albumin (HSA)
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Therapeutic: " Many tumor cell lines have since been shown to produce and secrete PDGF, some of which also express the cognate PDGF receptors; paracrine effect on the tumor stroma and, in some tumor cell lines, autocrine growth stimulation by PDGF are therefore possible; These DNA ligands therefore represent lead compounds for a novel class of high-affinity, specific antagonists of PDGF-AB and PDGF-BB."
Additional information: [3′T] represents a 3′-3′-linked thymidine nucleotide added to reduce 3′-exonuclease-mediated degradation
Reference (1996, Biochemistry ): Green, L. S., Jellinek, D., Jenison, R., Ostman, A., Heldin, C. H., & Janjic, N. (1996). Inhibitory DNA ligands to platelet-derived growth factor B-chain. Biochemistry, 35(45), 14413–14424. https://doi.org/10.1021/bi961544+
Aptamer: C2
Target: Human immunodeficiency virus type 1 Rev (HIV-1 Rev)
Type of nucleic acid: 2'-amino-RNA
Sequence: 5'GGAGGUCGACCUCGCGCGAGGAGGGUGGAGGGUCGUAGAGCGCGUAGGAGG3'
Sequence length: 51
GC content: 0.7058823529411765
Affinity: Kd: 19-36 nM
Pool type: 5'-GGGAGAUACCAGCUUAUUCAAUU-N71-AGAUAGUAAGUGCAAUCU-3'
Pool random region: 71
Binding buffer/conditions: 500 ul of 10 mM Hepes, pH 7.4/100 mM NaCl
Buffer type: Other Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic and Therapeutic: "RNA aptamers were selected to bind to the isolated Rev34_50 peptide. These results suggest that artificially selected binding cusps may have much in common with those found on natural molecules and have important implications for the development of novel diagnostic reagents and strategies for intracellular immunization"
Additional information: Pool was not stated, but I figured it out using the figures
Reference (1996, Proc Natl Acad Sci U S A ): Xu, W., & Ellington, A. D. (1996). Anti-peptide aptamers recognize amino acid sequence and bind a protein epitope. Proceedings of the National Academy of Sciences of the United States of America, 93(15), 7475–7480. https://doi.org/10.1073/pnas.93.15.7475
Aptamer: C8
Target: Human immunodeficiency virus type 1 Rev (HIV-1 Rev)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAUACCAGCUUAUUCAAUUGCUAGGCAAUGUUUCGGUUGGAGUAAUCCGGUGGCUUGCCAUGAUUUACGUGAGUGCUGAUCCGUGAUGAGAUAGUAAGUGCAAUCU3'
Sequence length: 110
GC content: 0.4545454545454545
Affinity: Kd: 19-36 nM
Pool type: 5'-GGGAGAUACCAGCUUAUUCAAUU-N71-AGAUAGUAAGUGCAAUCU-3'
Pool random region: 71
Binding buffer/conditions: 500 ul of 10 mM Hepes, pH 7.4/100 mM NaCl
Buffer type: Other Buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Diagnostic and Therapeutic: "RNA aptamers were selected to bind to the isolated Rev34_50 peptide. These results suggest that artificially selected binding cusps may have much in common with those found on natural molecules and have important implications for the development of novel diagnostic reagents and strategies for intracellular immunization"
Additional information: Pool was not stated, but I figured it out using the figures
Reference (1996, Proc Natl Acad Sci U S A ): Xu, W., & Ellington, A. D. (1996). Anti-peptide aptamers recognize amino acid sequence and bind a protein epitope. Proceedings of the National Academy of Sciences of the United States of America, 93(15), 7475–7480. https://doi.org/10.1073/pnas.93.15.7475