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
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
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
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
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
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
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
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
54,von Willebrand factor A1-domain,protein,P04275,Pr-DsDsDs-40,,1.03 nM,-8.987,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,Pr-DsDsDs-40 ( K D = 1.03 nM),step2c_literal_v3
664,PD-L1,protein,Q9NZQ7,8-60,,1.4 nM,-8.854,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,34711320,10.1016/j.aca.2021.339066,"8 e 60, a representative aptamer with high af fi nity (KD 1⁄4 1.4 nM determined by SPR)",elsevier_step2c
108,thrombin,protein,P00734,T.7,,1.5 nM,-8.824,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,SPR,,,binding buffer supplemented with 0.05% of Tween-20,,DNA,,37798416,10.1038/s41587-023-01973-8,T.7 exhibited the strongest binding signal with a 1.5 nM K d,step2c_literal_v3
337,human α-thrombin,protein,P00734,LOOPER modified thrombin aptamer,,1.6000000000000003e-09 M,-8.796,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,SPR,,,,,DNA,diversely functionalized; heteromultivalent,28938065,10.1021/jacs.7b07241,"Using single-cycle kinetics surface plasmon resonance (SPR), the LOOPER aptamer exhibited a Kd of 1.6 nM",step2c_acs_v1
316,CD44-HABD,protein,,Motif 4 (ADDA adduct),,2e-09 M,-8.699,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,,,,,,,,23057694,10.1021/bi300471d,motifs 2 and 4(ADDA adduct) have ~2 nM affinity to CD44-HABD,step2c_acs_v1
322,S-adenosylmethionine,protein,P17707,Bs SAM-I riboswitch,,3.0000000000000004e-09 M,-8.523,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,,,,,,,,23343213,10.1021/ja310742m,"Both μ MSA values agree well with results from the in-line probing assays performed using identical buffer conditions: ... 3 nM K d , respectively",step2c_acs_v1
323,S-adenosylmethionine,protein,P17707,Pi SAM-I riboswitch,,3.0000000000000004e-09 M,-8.523,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,,,,,,,,23343213,10.1021/ja310742m,which is on the order of the 3 nM value measured using a conventional inline probing assay,step2c_acs_v1
614,human α-Thrombin,protein,P00734,B1,,3.4 nM,-8.469,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,31129134,10.1016/j.ab.2019.05.012,"for MST the B aptamers (B1: 3.4 nM, B2: 5 nM, B3: 7.6 nM)",elsevier_step2c
338,human α-thrombin,protein,P00734,LOOPER modified thrombin aptamer,,4e-09 M,-8.398,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,,,,,,,,28938065,10.1021/jacs.7b07241,Preliminary binding analysis by label-free microscale thermophoresis showed a promising dissociation constant K d = 4 nM for thrombin,step2c_acs_v1
615,human α-Thrombin,protein,P00734,B2,,5.0 nM,-8.301,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,31129134,10.1016/j.ab.2019.05.012,"for MST the B aptamers (B1: 3.4 nM, B2: 5 nM, B3: 7.6 nM)",elsevier_step2c
710,sST2,protein,P30874,sS9_P,,5.6 nM,-8.252,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,37992929,10.1016/j.ijbiomac.2023.128295,"in case of sS9, parent aptamer has outperformed its truncated counterpart in terms of affinity as it has shown higher affinity (Kd ~5.6 nM).",elsevier_step2c
603,human α-Thrombin,protein,P00734,A2,,6.3 nM,-8.201,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,31129134,10.1016/j.ab.2019.05.012,for SCORE (b-nd analysis) the best are A2 (6.3 nM),elsevier_step2c
461,Lipopolysaccharide from Klebsiella pneumoniae ATCC 15380,protein,,aptamer seq. 5,,6.68e-09 M,-8.175,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,DPV,,,1 × PBS,,DNA,biotin,41323700,10.1039/d5ra06759f,The binding affinity of aptamer seq. 5 was 6.68 nM (Fig. 9C).,step2c_acs_v1
609,human α-Thrombin,protein,P00734,A3,,6.9 nM,-8.161,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,31129134,10.1016/j.ab.2019.05.012,for SCORE (b-nd analysis) the best are A2 (6.3 nM) and A3 (6.9 nM),elsevier_step2c
139,PTK7,protein,Q13308,4AsF,,7.2 nM,-8.143,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,SPR,310.15,7.4,1 × DPBS,5.0,DNA,"SF at positions A23, A24, A25, A26",41065179,10.1021/jacs.5c11823,"4AsF, which exhibited a 10-fold reduction compared to 4APS (0.77 vs 7.20 nM)",step2c_literal_v3
556,VEGF165,protein,P15692,cot-pega,,7.33 nM,-8.135,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,26956592,10.1016/j.jconrel.2016.03.006,The K D of cot-pega for VEGF was 7.33 nM (Fig. 1b),elsevier_step2c
616,human α-Thrombin,protein,P00734,B3,,7.6 nM,-8.119,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,31129134,10.1016/j.ab.2019.05.012,"for MST the B aptamers (B1: 3.4 nM, B2: 5 nM, B3: 7.6 nM)",elsevier_step2c
605,human α-Thrombin,protein,P00734,A3,,8.0 nM,-8.097,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,31129134,10.1016/j.ab.2019.05.012,For BLI it was found that aptamer A3 (8 nM and 25.5 nM) is the best binder,elsevier_step2c
348,NP,protein,Q16612,NP-C04,,8.1e-09 M,-8.092,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,,7.4,"20 mM HEPES, 150 mM NaCl, 2 mM KCl, 2 mM MgCl2, and 2 mM CaCl2 (pH 7.4)",,DNA,FAM,30740973,10.1021/acs.analchem.8b04623,"the K d values of NP-D01, NP-C04, and NP-D02 were 76..1 ± 10.9, 8.1 ± 2.4, and 41.3 ± 9.5 nM, respectively.",step2c_acs_v1
92,Okadaic Acid,protein,O95232,OA-LC2-TF,,8.735 nM,-8.059,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,7.5,"50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5)",2.0,DNA,terminal fixation with GC-rich sequences,36322695,10.1021/acs.analchem.2c02653,The terminal-fixed OA-LC2 (OA-LC2-TF) exhibited a K d of 8.735 ± 0.606 nM,step2c_literal_v3
423,TAR RNA,protein,Q13395,TAR RNA aptamer (best binding),,9.000000000000001e-09 M,-8.046,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,,,,,,,,39167715,10.1021/jacs.4c08824,A Biolayer Interferometry (BLI) experiment revealed that TAR RNA aptamers with the best binding affinity exhibited the dissociation constant ( K D) at 9 nM,step2c_acs_v1
613,human α-Thrombin,protein,P00734,B1,,9.2 nM,-8.036,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,31129134,10.1016/j.ab.2019.05.012,For SCORE (Anabel analysis) the best is B1 (9.2 nM),elsevier_step2c
345,streptavidin,protein,,S8,,1e-08 M,-8.0,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,,,,,,,,30520292,10.1021/acssensors.8b00945,"At pH 7.4, we determined that S8 has a K d of 10 nM",step2c_acs_v1
366,trastuzumab,protein,Q9ULR3,CH1S-3,,1.0300000000000001e-08 M,-7.987,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,MST,298.15,,washing bu ff er with the addition of 0.005% Tween 20,,DNA,5'-Cy5,32516525,10.1021/jacs.9b13370,a ffi nity with a K d value of aptamer CH1S-3 of 10.3 nM,step2c_acs_v1
334,17 β -Estradiol,protein,P42167,22-mer aptamer,,1.1000000000000001e-08 M,-7.959,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,,,,,,,,25803717,10.1021/acs.analchem.5b00335,new 35-mer and 22-mer aptamers were generated with K D ' s of 14 and 11 nM,step2c_acs_v1
557,25-HydroxyvitaminD3,protein,A0A0C5B5G6,VDBA14,,11.0 nM,-7.959,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,27520502,10.1016/j.bios.2016.08.011,the dissociation constants (Kd) of the VDBA14 was estimated to be 11 nM based on a non-linear regression method.,elsevier_step2c
572,CTLA-4,protein,P16410,aptCTLA-4,,11.84 nM,-7.927,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,28918052,10.1016/j.omtn.2017.08.006,dissociation constant (Kd) being 11.84 nM,elsevier_step2c
101,thrombin,protein,P00734,Uyne A - AUyne,,12.16 nM,-7.915,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,,"buffer used for the bead-based selection, which contains Tween-20",,DNA,5-ethynyl-2′-deoxyuridine (Uyne); Biotin (5' end),37531184,10.1021/acschembio.3c00183,U yne A - AUyne | 12.16 ± 0.02,step2c_literal_v3
711,sST2,protein,P30874,sS9_P,,13.0 nM,-7.886,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,37992929,10.1016/j.ijbiomac.2023.128295,The best performing aptamer candidate sS9_P (80mer) has shown affinity in low nanomolar range (~5.6 nM in ALISA and ~13 nM in ITC),elsevier_step2c
631,Bisphenol A,protein,O75897,38-mer BPA aptamer,,13.17 nM,-7.88,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,32113141,10.1016/j.foodchem.2020.126459,"The K d values of the 63-mer, 38-mer, 12-mer and 23-mer aptamers were determined by using MST experiments, which were 491.69 nM, 13.17 nM, 27.05 nM and 1190.61 nM",elsevier_step2c
100,thrombin,protein,P00734,Uyne A - Uyne Uyne,,13.96 nM,-7.855,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,,"buffer used for the bead-based selection, which contains Tween-20",,DNA,5-ethynyl-2′-deoxyuridine (Uyne); Biotin (5' end),37531184,10.1021/acschembio.3c00183,U yne A - U yne U yne | 13.96 ± 0.03,step2c_literal_v3
333,17 β -Estradiol,protein,P42167,35-mer aptamer,,1.4000000000000001e-08 M,-7.854,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,,,,,,,,25803717,10.1021/acs.analchem.5b00335,new 35-mer and 22-mer aptamers were generated with K D ' s of 14 and 11 nM,step2c_acs_v1
641,hexahistidine peptide,protein,,AptHis-1,,15.0 nM,-7.824,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,32739349,10.1016/j.ab.2020.113893,the Kd was as low as 15 nM (Table S1),elsevier_step2c
642,hexahistidine peptide,protein,,AptHis-2,,15.0 nM,-7.824,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,32739349,10.1016/j.ab.2020.113893,the Kd was as low as 15 nM (Table S1),elsevier_step2c
643,hexahistidine peptide,protein,,AptHis-3,,15.0 nM,-7.824,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,32739349,10.1016/j.ab.2020.113893,the Kd was as low as 15 nM (Table S1),elsevier_step2c
95,Dinophysistoxin,protein,,DTX-SL1-TF,,15.45 nM,-7.811,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,BLI,,7.5,"50 mM Tris, 150 mM NaCl, 2 mM MgCl2, and 0.02% Tween-20 (pH 7.5)",2.0,DNA,terminal fixation,36322695,10.1021/acs.analchem.2c02653,DTX-SL1-TF showed a K d of 15.45 ± 1.92 nM,step2c_literal_v3
612,human α-Thrombin,protein,P00734,B1,,15.7 nM,-7.804,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,31129134,10.1016/j.ab.2019.05.012,"for SPR A2, B1 and B3 lay in the upper range (17 nM, 15.7 nM, 17.6 nM)",elsevier_step2c
604,human α-Thrombin,protein,P00734,A2,,17.0 nM,-7.77,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,31129134,10.1016/j.ab.2019.05.012,"for SPR A2, B1 and B3 lay in the upper range (17 nM, 15.7 nM, 17.6 nM)",elsevier_step2c
617,human α-Thrombin,protein,P00734,B3,,17.6 nM,-7.754,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_supp,,,,,,text,,,,31129134,10.1016/j.ab.2019.05.012,"for SPR A2, B1 and B3 lay in the upper range (17 nM, 15.7 nM, 17.6 nM)",elsevier_step2c