RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: Clone 10
Target: Protein kinase C beta II (protein kinase C βII)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGAAUUCCGACCAGAGGUUGUUAAGUGCGAGUUGUUUUACUCCGAUGAUACGGGGAGCGUUAGAGUCUUAUGACCUUGUUCUCCACGUCACUGUCCAAGUCACUCCGCGUCAUAGCAGUCGGAUCCUGUACAUAUGUGCGUCUACAUGGAUCCUCA3'
Sequence length: 159
GC content: 0.4968553459119497
Affinity: Kd: 7 nM
Pool type: 5'-GGGAGAAUUCCGACCAGAGGCUU-N120-CAUAUGUGCGUCUACAUGGAUCCUCA-3'
Pool random region: 120
Binding buffer/conditions: 20 mM HEPES, pH 7.5, 10 mM MgCl,, 0.3 m~ CaCl,, 1 mM DTT, 0.05 m~ ATP
Divalent salt: MgCl/CaCl
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: Not applicable
Application as quoted in the referenced paper: Detection: " This work opens the possibility that the substrate recognition properties conferred on most proteins by natural selection can be mimicked by artificial evolution and that new allosteric inhibitors and activators of enzymes may be found using in vitro selection. As a practical example, expression of these aptamers in cells should now allow inhibition of one specific protein kinase C isozyme, thus opening the possibility for dissecting the roles of protein kinase C isozymes in signal transduction."
Additional information: Paper says RNA aptamers but reports the sequences in DNA so T's were changed to U's in the spreadsheet
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 (1994, J Biol Chem ): Conrad R, Keranen LM, Ellington AD, Newton AC. Isozyme-specific inhibition of protein kinase C by RNA aptamers. J Biol Chem. 1994 Dec 23;269(51):32051-4. PMID: 7528207
Aptamer: 100
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAACCGGUAGUCGCAUGGCCCAUCGCGCCCGGUUCGACAUGAGGCCCGGAUCCGGC3'
Sequence length: 76
GC content: 0.6447368421052632
Affinity: Kd1: 0.20 ± 0.02 nM
Kd2: 42 ± 30 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: 100t
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGCCGGUAGUCGCAUGGCCCAUCGCGCCCGG3'
Sequence length: 31
GC content: 0.7741935483870968
Affinity: Kd1: 0.42 ± 0.04 nM
Kd2: 182 ±94 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 
Post-SELEX modifications: Truncated
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: 44t
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGAAGCUUGAUGGGUGACACACGUCAUGCCGAGCU3'
Sequence length: 35
GC content: 0.5714285714285714
Affinity: Kd1: 0.48 ± 0.04 nM
Kd2: 82 ± 23 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 
Post-SELEX modifications: Truncated
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: 12t
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGAAGGGAACCUGCGUCUCGGCACCUUCG3'
Sequence length: 29
GC content: 0.6551724137931034
Affinity: Kd1: 1.1 ±0.2 nM
Kd2: 180 ± 160 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 
Post-SELEX modifications: Truncated
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: 40t
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGUCAACGGUUGAGUCUGUCCCGUUCGAC3'
Sequence length: 29
GC content: 0.5862068965517241
Affinity: Kd1: 20 ± 1 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 
Post-SELEX modifications: Truncated
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: 84t
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGCUCAAUAGUUGGAGGCCUGUCCUCGCCGUAGAGC3'
Sequence length: 36
GC content: 0.6111111111111112
Affinity: Kd1:1.8 ±0.4 nM
Kd2: 31 ± 10 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 
Post-SELEX modifications: Truncated
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: 126t
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGAACGGUUCUGUGUGUGGACUAGCCGCGGCCGUU3'
Sequence length: 35
GC content: 0.6285714285714286
Affinity: Kd1: 1.4 ±0.2 nM
Kd2: 181 ± 57 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 
Post-SELEX modifications: Truncated
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: 44
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAAAGCUUGAUGGGUGACACACGUCAUGCCGAGCUUUUCGACAUGAGGCCCGGAUCCGGC3'
Sequence length: 80
GC content: 0.5625
Affinity: Kd1: 1.7 ±0.5 nM
Kd2: 38 ±32 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: 12
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAAGCAGACGAAGGGAACCUGCGUCUCGGCACCUUCGACAUGAGGCCCGGAUCCGGC3'
Sequence length: 77
GC content: 0.6103896103896104
Affinity: Kd1: 0.48 ± 0.07 nM
Kd2: 21 ±5 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: 40
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAAGCUUGAUGGGUGACACACGUCAUGCCGAGCUUCGACAUGAGGCCCGGAUCCGGC3'
Sequence length: 77
GC content: 0.5844155844155844
Affinity: Kd1: 0.19 ±0.09 nM
Kd2: 10 ± 1 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: 84
Target: Vascular Endothelial Growth Factor (VEGF)
Type of nucleic acid: ssRNA
Sequence: 5'GGGAGCUCAGAAUAAACGCUCAAGCUCAAUAGUUGGAGGCCUGUCCUCGCCGUAGAGCGUUCGACAUGAGGCCCGGAUCCGGC3'
Sequence length: 83
GC content: 0.5903614457831325
Affinity: Kd1: 0.82 ±0.2 nM
Kd2: 21 ± 5 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