id,target_name_canonical,target_type,target_uniprot,aptamer_name,aptamer_seq,kd_reported,kd_log10_molar,measurement_class,binding_constant_type,tier,source_origin,verification_level,sequence_status,seq_source,pi_provenance_flag,assay_method,assay_temperature_k,assay_ph,assay_buffer,assay_cations,aptamer_chemistry,aptamer_modifications,source_pmid,doi,verbatim_quote,source_db
188,PDGF-BB,protein,P01127,36aApt,,0.036 pM,-13.444,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,ELISA,298.0,,,,DNA,,28825469,10.1021/acscombsci.6b00163,36aApt | 0.036 ± 0.012 | - 18.33,step2c_literal_v3
186,PDGF-BB,protein,P01127,38aApt,,0.094 pM,-13.027,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,ELISA,298.0,,,,DNA,,28825469,10.1021/acscombsci.6b00163,38aApt | 0.094 ± 0.008 | - 17.76,step2c_literal_v3
44,IL-8,protein,P10145,8A-35,GGGGGCUUAUCAUUCCAUUUAGUGUUAUGAUAACC,1.72e-12 M,-11.764,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.0,7.4,"HBST running buffer (10 mM HEPES, pH 7.4, 150 mM NaCl, and 0.005% Tween 20)",,2'F-RNA,2'-fluoro-pyrimidine modified,24129312,10.1016/j.biomaterials.2013.09.107,| 8A-35       | 5.78 x 10 4 | 9.95 x 10 -8 | 1.72 x 10 -12 | 2.80         | 3.11 x 10 1  |,step2c_literal_v3
598,human α-Thrombin,protein,P00734,A1,,2.0 pM,-11.699,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,31129134,10.1016/j.ab.2019.05.012,"Also for aptamer A1 we measured with MST KD values in the pico- and nanomolar range (2 pM and 52 nM). The lowest KD value is determined with MST (shown as bar) for aptamer A1, which is 2 pM.",elsevier_step2c
621,nucleolin,protein,P19338,Cy5-AT11-B0,TGGTGGTGGTTGGTGGTGGTGGTGGT,3.3e-12 M,-11.481,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,text,,,,31301466,10.1016/j.ijpharm.2019.118511,yielding K D values of 5.2 × 10 -12 and 3.3 × 10 -12 M for Cy5-AT11 G4 C8 and Cy5-AT11-B0 G4 C8,elsevier_step2c
620,nucleolin,protein,P19338,Cy5-AT11,TGGTGGTGGTTGTTGTGGTGGTGGTGGT,5.2e-12 M,-11.284,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,text,,,,31301466,10.1016/j.ijpharm.2019.118511,yielding K D values of 5.2 × 10 -12 and 3.3 × 10 -12 M for Cy5-AT11 G4 C8 and Cy5-AT11-B0 G4 C8,elsevier_step2c
184,PDGF-BB,protein,P01127,FullApt,,5.33 pM,-11.273,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,ELISA,298.0,,,,DNA,,28825469,10.1021/acscombsci.6b00163,FullApt | 5.33 ± 2.36 | - 15.37,step2c_literal_v3
185,PDGF-BB,protein,P01127,40Apt,,5.92 pM,-11.228,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,ELISA,298.0,,,,DNA,,28825469,10.1021/acscombsci.6b00163,40Apt | 5.92 ± 1.13 | - 15.31,step2c_literal_v3
187,PDGF-BB,protein,P01127,38bApt,,7.03 pM,-11.153,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,ELISA,298.0,,,,DNA,,28825469,10.1021/acscombsci.6b00163,38bApt | 7.03 ± 1.28 | - 15.21,step2c_literal_v3
618,nucleolin,protein,P19338,Cy5-AT11,TGGTGGTGGTTGTTGTGGTGGTGGTGGT,9.1e-12 M,-11.041,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,text,,,,31301466,10.1016/j.ijpharm.2019.118511,K D values of 9.1 × 10 -12 and 9.5 × 10 -12 M for Cy5-AT11 G4 and Cy5-AT11-B0 G4,elsevier_step2c
619,nucleolin,protein,P19338,Cy5-AT11-B0,TGGTGGTGGTTGGTGGTGGTGGTGGT,9.5e-12 M,-11.022,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,text,,,,31301466,10.1016/j.ijpharm.2019.118511,K D values of 9.1 × 10 -12 and 9.5 × 10 -12 M for Cy5-AT11 G4 and Cy5-AT11-B0 G4,elsevier_step2c
269,thrombin,protein,P00734,HD1-12A-DAB,,13.1 pM,-10.883,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,filter_binding,,,selection buffer,,DNA,,41053535,10.1002/advs.202509867,HD1-12A-DAB EXACT inhibitor bound to thrombin and prothrombin with K D s of 13.1 pm,step2c_literal_v3
143,P-selectin,protein,Q14242,PF377,,14.0 pM,-10.854,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377 | 14,step2c_literal_v3
147,P-selectin,protein,Q14242,PF377sl,,14.0 pM,-10.854,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,296.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377sl | 14,step2c_literal_v3
142,P-selectin,protein,Q14242,PF377,,16.0 pM,-10.796,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377 | 16,step2c_literal_v3
144,P-selectin,protein,Q14242,PF377,,18.0 pM,-10.745,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,277.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377 | 18,step2c_literal_v3
623,Malate Synthase,protein,Q8N0X4,MS10-Trunc,GGTGGTGGTGG,19.0 pM,-10.721,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,abstract,,,,31704587,10.1016/j.omtn.2019.09.026,MS10-Trunc aptamer exhibited high af fi nity for MS (equilibrium dissociation constant [KD]  19 pM),elsevier_step2c
140,PDGF-C,protein,P01127,α-PC,CTACTGTGTGATGTCTGAGAGCAGCGTCTAAACGAACAAGCGAACCTATGCACAGAGGACAGTACATCAGACAC,20.0 pM,-10.699,intrinsic,KD,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,,7.4,"HBS-EP + (10-mM HEPES, 150-mM NaCl, 3-mM EDTA, and 0.05% Tween 20, pH 7.4)",,DNA,PEG,42138517,10.1167/iovs.67.5.36,SPR analysis demonstrated that the α -PC aptamer bound tightly to PDGF-C with a dissociation constant ( KD ) of 20 pM,step2c_literal_v3
146,P-selectin,protein,Q14242,PF377sl,,29.0 pM,-10.538,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377sl | 29,step2c_literal_v3
669,bevacizumab,protein,P31995,A14#1,GCGGTTGGTGGTAGTTACGTTCGC,44.0 pM,-10.357,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,abstract,,,,35114463,10.1016/j.bios.2022.114027,affinity of A14#1 to bevacizumab markedly increased at pH 4.7 ( K D = 44 pM),elsevier_step2c
145,P-selectin,protein,Q14242,PF377sl,,46.0 pM,-10.337,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377sl | 46,step2c_literal_v3
148,P-selectin,protein,Q14242,PF373sl,,56.0 pM,-10.252,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF373sl | 56,step2c_literal_v3
56,von Willebrand factor A1-domain,protein,P04275,Rn-DsDsDs-53mh,,61.3 pM,-10.213,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,SPR,310.15,,1 × PBS supplemented with 0.05% (w/v) Nonidet P-40,,DNA,"Ds (7-(2-thienyl)imidazo[4,5b]pyridine); mini-hairpin DNA",27966933,10.1021/jacs.6b10767,RnDsDsDs-53mh ( K D = 61.3 pM),step2c_literal_v3
542,Myoglobin,protein,P02144,anti-Mb aptamer,,65.0 pM,-10.187,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,25957831,10.1016/j.bios.2015.04.089,"The corresponding af fi nity, K D, values calculated from the ratio between dissociation ( k d) and association ( k a ) was found to be  65 pM.",elsevier_step2c
53,von Willebrand factor A1-domain,protein,P04275,Rn-DsDsDs-44,,74.9 pM,-10.126,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,SPR,310.15,,1 × PBS supplemented with 0.05% (w/v) Nonidet P-40,,DNA,"Ds (7-(2-thienyl)imidazo[4,5b]pyridine)",27966933,10.1021/jacs.6b10767,Rn-DsDsDs-44 ( K D = 74.9 pM) exhibited the highest a ffi nity,step2c_literal_v3
152,PDGF-BB,protein,P01127,PDGF-B aptamer,,0.1 nM,-10.0,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,,,,,DNA,2'-fluoro; 2'-O-methyl; hexaethylene glycol spacer; inverted 3'-3' thymidine cap; 40-kd PEG conjugated,9916931,10.1016/S0002-9440(10)65263-7,the binding affinity of the aptamer used in the experiments described below ( K d ≈ 0.1 nM),step2c_literal_v3
547,ofloxacin,protein,Q9H015,Q2,ATACCAGCTTATTCAATTGCAGGGTATCTGAGGCTTGATCTACTAAATGTCGTGGGGCATTGCTATTGGCGTTGATACGTACAATCGTAATCAGTTAG,0.11 nM,-9.959,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,text,,,,26547431,10.1016/j.bios.2015.10.069,Their K D values were calculated at K D 1⁄4 0.11 nM ( 7 0.06) for aptamer Q2,elsevier_step2c
245,MPO,protein,P05164,MPO-16,GTCTGGAAACGACGAGGGCCACTGATTAACGTAGTTAATTGGTCTTGTCG,166.0 pM,-9.78,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,backfill_text_verified,,flow_cytometry,,,"selection buffer (DPBS with 2.5 mM MgCl2 , 1 mM CaCl 2 , 0.01% TWEEN-20, 0.2% BSA)",2.5,DNA,,37277648,10.1038/s41557-023-01207-z,MPO16 revealed the highest binding affinity ( K d = 166 pM),step2c_literal_v3
149,P-selectin,protein,Q14242,PF398sl,,178.0 pM,-9.75,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF398sl | 178,step2c_literal_v3
57,von Willebrand factor A1-domain,protein,P04275,Rn-DsDs-51mh2,,182.0 pM,-9.74,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,SPR,310.15,,1 × PBS supplemented with 0.05% (w/v) Nonidet P-40,,DNA,"Ds (7-(2-thienyl)imidazo[4,5b]pyridine); mini-hairpin DNA",27966933,10.1021/jacs.6b10767,Rn-DsDs-51mh2 ( K D = 182 pM),step2c_literal_v3
548,ofloxacin,protein,Q9H015,Q8,ATACCAGCTTATTCAATTAGTTGTGTATTGAGGTTTGATCTAGGCATAGTCAACAGAGCACGATCGATCTGGCTTGTTCTACAATCGTAATCAGTTAG,0.2 nM,-9.699,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,text,,,,26547431,10.1016/j.bios.2015.10.069,K D 1⁄4 0.20 nM ( 7 0.09) for aptamer Q8,elsevier_step2c
558,OH-BDE47,protein,,BDE-A-8,GACAGCCGGGGCATCAGAGCAGCCGATTGTCTGTTGTGCC,0.2 nM,-9.699,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,text,,,,27566357,10.1016/j.aca.2016.06.040,"The dissociation constant (Kd) of BDE-A-8 and BDE-A-12 were 0.20 nM (~0.08 ppb) and 1.53 nM (~0.8 ppb), respectively, in PBS buffer condition.",elsevier_step2c
234,MPO,protein,P05164,MPO-02,TATGCGATTTCAAAAATGTTACGATGGATATTGACATTTAAATATGTCGG,227.0 pM,-9.644,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,backfill_text_verified,,flow_cytometry,,,"selection buffer (DPBS with 2.5 mM MgCl2 , 1 mM CaCl 2 , 0.01% TWEEN-20, 0.2% BSA)",2.5,DNA,,37277648,10.1038/s41557-023-01207-z,MPO-02 ... 227,step2c_literal_v3
307,P-selectin,protein,Q14242,PF377sl,,250.0 pM,-9.602,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,flow_cytometry,296.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377sl | 250,step2c_literal_v3
639,thrombin,protein,P00734,29-mer thrombin-specific aptamer,AGTCCGTGGTAGGGCAGGTTGGGGTGACT,298.0 pM,-9.526,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,text,,,,32570818,10.3390/s20123442,The n-curve analysis provided a Kd of 298 pM ( + 111 / 81 pM),elsevier_step2c
660,20 Methyl Spirolide G,protein,,SPX 7,GGCGGTGTGGGTACCACGAGGTTTGGACGCGCGTAGCACCCCATTCAGC,3e-10 M,-9.523,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,text,,,,34144421,10.1016/j.foodchem.2021.130332,"The present study, among the aptamers selected, the aptamer with highest affinity had a dissociation constant of 0.3 nM for SPX G",elsevier_step2c
554,chimeric-tPA,protein,,Chi-tPA 1,TTCCAACGGTTGGTGGGTGGTT,0.32 nM,-9.495,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,abstract,,,,26876003,10.1016/j.pep.2016.02.004,selected aptamer having KD values of 0.320 nM,elsevier_step2c
55,von Willebrand factor A1-domain,protein,P04275,ARC1172-41,,326.0 pM,-9.487,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,SPR,310.15,,1 × PBS supplemented with 0.05% (w/v) Nonidet P-40,,DNA,,27966933,10.1021/jacs.6b10767,ARC1172-41 ( K D = 326 pM),step2c_literal_v3
247,Human thrombin,protein,P00734,Lin08-08,,0.4 nM,-9.398,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Lin(08-08) | 1.63 10^6 | 6.94 10^-4 | 0.4,step2c_literal_v3
249,Human thrombin,protein,P00734,Pse08-08,,0.4 nM,-9.398,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Pse(08-08) | 1.19 10^6 | 5.10 10^-4 | 0.4,step2c_literal_v3
50,PDGF-BB,protein,P01127,PDGF-specific aptamer,,5e-10 M,-9.301,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,microcantilever,310.15,7.4,"PBSM buffer (10.1 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, and 1 mM MgCl2, pH 7.4)",1.0,DNA,3'-3'-linked thymidine nucleotide ([3'T]); thiolated 5'-end,24723743,10.1016/j.snb.2012.02.045,"K d , as shown in Fig. 10, decreased from approximately 12 × 10 -10 M to 5 × 10 -10 M as the temperature changed from 19 to 37 ◦ C.",step2c_literal_v3
173,human α-thrombin,protein,P00734,Apt29,AGTCCGTGGTAGGGCAGGTTGGGGTGACT,0.5 nM,-9.301,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,,,,,,DNA,,28763192,10.1021/acs.analchem.7b02313,"a 29nucleotide aptamer (5 ′ -AGT CCG TGG TAG GGC AGG TTG GGG TGA CT-3 ′ , denoted as Apt29 here) binds to the heparin-binding site of human α -thrombin with a dissociation constant ( K d) around 0.5 nM.",step2c_literal_v3
205,thrombin,protein,P00734,TBA29,,0.5 nM,-9.301,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,,31614078,10.1021/acs.analchem.9b03368,The 29-nt TBA29 aptamer has a bimodular duplex-antiparallel G4 structure and binds to thrombin with a binding a ffi nity of 0.5 nM. 30,step2c_literal_v3
550,Thrombin,protein,P00734,TBA29,,5e-10 M,-9.301,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,26643617,10.1016/j.jconrel.2015.11.028,and TBA29 (~5 × 10 -10 M),elsevier_step2c
530,AGEs-HSA,protein,,#9s,TCTGCCACCCTCCGACTAACATATCCGGCCTGAGACCA,0.57 nM,-9.244,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,backfill_text_verified,,,,,abstract,,,,24012635,10.1016/j.mvr.2013.08.010,"Surface plasmon resonance analysis revealed that K D values of #4s, #7s and #9s were 0.63, 0.36, and 0.57 nM, respectively.",elsevier_step2c
175,human α-thrombin,protein,P00734,5'-TMR-Apt15-T24,GGTTGGTGTGGTTGG,0.6 nM,-9.222,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,backfill_text_verified,,CE-LIF,298.15,7.5,sample bu ff er containing 10 mM Tris-HCl (pH 7.5) and 5 mM KCl,,DNA,TMR label at 5'-end; polyT tail (24 T) at 3'-end,28763192,10.1021/acs.analchem.7b02313,0.6 nM for 5 ′ -TMR-Apt15-T24,step2c_literal_v3
176,human α-thrombin,protein,P00734,5'-TMR-Apt15-T25,GGTTGGTGTGGTTGG,0.6 nM,-9.222,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,backfill_text_verified,,CE-LIF,298.15,7.5,sample bu ff er containing 10 mM Tris-HCl (pH 7.5) and 5 mM KCl,,DNA,TMR label at 5'-end; polyT tail (25 T) at 3'-end,28763192,10.1021/acs.analchem.7b02313,0.6 nM for 5 ′ -TMR-Apt15-T25,step2c_literal_v3
303,EGFR,protein,P00533,Anti-EGF receptor aptamer,,0.62 nM,-9.208,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,3' end sulfhydryl group (-SH),41877526,10.1021/acs.molpharmaceut.5c01966,"Anti-EGF receptor aptamers ( K d : 0.62 nM, DNA aptamers)",step2c_literal_v3
529,AGEs-HSA,protein,,#4s,CAGAATCGGGGACCACGACACTGCACATACCTCGTACGAA,0.63 nM,-9.201,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,backfill_text_verified,,,,,abstract,,,,24012635,10.1016/j.mvr.2013.08.010,"Surface plasmon resonance analysis revealed that K D values of #4s, #7s and #9s were 0.63, 0.36, and 0.57 nM, respectively.",elsevier_step2c
154,thrombin,protein,P00734,HD1-22,GGTTGGTGTGGTTGGAAAAAAAAAAAAGTCCGTGGTAGGGCAGGTTGGGGTGACT,6.5e-10 M,-9.187,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,,,,,DNA,bivalent fusion; poly-dA linker,18826387,10.1111/j.1538-7836.2008.03162.x,HD1-22 | Thrombin | K D ( M) | 6.5 · 10 ) 10,step2c_literal_v3