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
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
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
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
331,MutS,protein,O15457,2-06,ACTTCTGCCCGCCTCCTTCCTGGTAAAGTCATTAATAGGTGTGGGGTGCCGGGCATTTCGGAGACGAGATAGGCGGACACT,1.23e-10 M,-9.91,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,25668425,10.1021/acs.analchem.5b00171,The best fi t was obtained at K d = 123 pM and [T]0 = 213 pM,step2c_acs_v1
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
363,HBcAg,protein,,A-9,AGCAGCACAGAGGTCAGATGAGGCCTGGTGATCGTGCCCAGGCCATATGAGCAAGGAACCCCTATGCGTGCTACCGTGAA,2.0000000000000003e-10 M,-9.699,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,affinity_real_time_qPCR,,,,,DNA,,32250595,10.1021/acs.analchem.9b05740,This aptamer showed strong binding to HBcAg ( K d : 0.2 nM),step2c_acs_v1
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
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
318,VEGF165,protein,P15692,3R02,TGTGGGGGTGGACTGGGTGGGTACC,3e-10 M,-9.523,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,23237717,10.1021/ac303023d,The K d value for 3R02 was 300 pM,step2c_acs_v1
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
478,FLRPp (O serotype),protein,,FMD_1,,3.46e-10 M,-9.461,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,SPR,,,,,DNA,,42010751,10.1021/acs.analchem.5c04748,dissociation constants ( KD ) of 3.46 × 10 -10 M,step2c_acs_v1
358,HBeAg,protein,,EAg3-Py,TTTTTTTTGGGCGAAGACCGGGACGGGAGGAAAGAGATGTTTGGTTTT,4.0000000000000007e-10 M,-9.398,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,affinity_real_time_qPCR,,7.4,"1 × BB (50 mM Tris-HCl (pH 7.4), 5 mM KCl, 50 mM NaCl, 7 mM MgCl2, and 0.05% Tween 20)",,DNA,pyrrolo-dC,32250595,10.1021/acs.analchem.9b05740,The K d value is 0.4 nM for the HBeAg complex with the pyrrolo-dC modi fi ed aptamer EAg3,step2c_acs_v1
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
415,BDNF,protein,P23560,NV_B12,GGATTTGAGCTTATGTGGCATAGGTTGCCTGGGTGGGTGGGGTCGGGGAA,5e-10 M,-9.301,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,ALISA,,,1 × selection buffer,,DNA,biotin,38149631,10.1021/acschemneuro.3c00661,"The equilibrium dissociation constant ( K d) for the NV_B12/BDNF interaction was obtained by fitting the equation, Y = B max × X /( K d + X )... The K d value determined to be 0.5 nM (95% CI: 0.4 -0.6 nM)",step2c_acs_v1
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
343,PlanarAu,protein,,1N,TATGCATGTGTAGTAAGACCTAGTCCACAATCAACG,5.600000000000001e-10 M,-9.252,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,QCM,,,AIB,,DNA,,30189130,10.1021/acscombsci.8b00048,aptamer 1N showing the highest affinity (0.56 nM),step2c_acs_v1
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
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
332,MutS,protein,O15457,2-06,ACTTCTGCCCGCCTCCTTCCTGGTAAAGTCATTAATAGGTGTGGGGTGCCGGGCATTTCGGAGACGAGATAGGCGGACACT,6.5e-10 M,-9.187,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,25668425,10.1021/acs.analchem.5b00171,The experimental points from the second step resulted in the best fi t with the theoretical dependence of R versus [L] 0 at K d = 650 pM,step2c_acs_v1
536,tetracycline,protein,Q14728,TC aptamer,,770.0 pM,-9.114,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,25517161,10.1016/j.bpj.2014.11.001,dissociation constant Kd of 770 pM ([Mg 2 þ ] 1⁄4 10 mM),elsevier_step2c
459,PSMA,protein,Q04609,C3,,8.000000000000001e-10 M,-9.097,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,EMSA,,,5 mM Mg2+,,DNA,phenol-dT; naphthyl-dC; PSMA-617 bait,41126016,10.1021/jacs.5c13307,an exemplar shows very high affinity for PSMA ( K d ∼ 0.8 nM).,step2c_acs_v1
634,Immunoglobulin E,protein,Q96D42,IgE37-T10-FAM,GGGGCACGTTTATCCGTCCCTAGTGGCGTGCCCC,0.8 nM,-9.097,intrinsic,Kd,Gold,elsevier,extraction_verified,verified_in_text_or_SI,original,,,,,abstract,,,,32498825,10.1016/j.talanta.2020.121018,The FA assay using T10-labeled aptamer with a dissociation constant ( K d) about 0.8 nM,elsevier_step2c
33,Tasset - thrombin complex,protein,,Bock,GGTTGGTGTGGTTGG,0.87 nM,-9.06,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,BSI,283.15,7.5,50 mM TRIS buffer (pH 7.5) containing 100 mM NaCl and 1 mM MgCl2,1.0,DNA,,22032342,10.1021/ac202823m,Bock - [Tasset complex] | not available | 0.87 ( 0.18 nM,step2c_literal_v3
38,alpha-thrombin,protein,P05154,RNAR9D-14T,GGCGGUCGAUCACACAGUUCAAACGUAAUAAGCCAAUGUACGAGGCAGACGACUCGCC,1.0 nM,-9.0,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,filter_binding,310.15,7.4,Hepes-saline buffer with 0.01% BSA,,2'F-RNA,2' Fluorocytosine; 2' Fluorouracil,22385910,10.1111/j.1538-7836.2012.04679.x,Nitrocellulose filter binding indicates that RNAR9D-14T binds with high affinity to both human prothrombin (apparent K d =10 nM) and α-thrombin (apparent Kd =1 nM),step2c_literal_v3
150,P-selectin,protein,Q14242,PF422sl,,1000.0 pM,-9.0,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,PF422sl | 1 X 103,step2c_literal_v3
398,neomycin,protein,Q96LI5,Aptamer A,GGACUGGGCGAGAAGUUUAGUCC,1e-09 M,-9.0,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,36453647,10.1021/acschembio.2c00653,The binding affinity of neomycin to Aptamer A shows a strong K d  of 1 nM with an enthalpy and entropy value of -100 kJ/mol & -163.1 J/mol. K,step2c_acs_v1
432,Sc3+,protein,Q96PL5,Sc-1,CTCTCGACGACGGACCATTCCCGTGGAATGACTACGTATATGTCGTC,1e-09 M,-9.0,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,fluorescence,,,SELEX buffer,,DNA,,39743479,10.1021/jacs.4c13768,true K d for the binding of Sc-1 to Sc 3+ to be 1.0 nM,step2c_acs_v1
458,PSMA,protein,Q04609,C3 (without fluorescein),,1e-09 M,-9.0,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,EMSA,,,,,DNA,phenol-dT; naphthyl-dC; Cy5 label,41126016,10.1021/jacs.5c13307,"EMSA data show that Cy5-labeled C3 without fluorescein binds PSMA just as strongly as the parent construct, with an apparent K d of ∼ 1 nM (Figure S9).",step2c_acs_v1