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
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
406,SARS-CoV-2 spike protein (wild type),protein,,DSA1N5,,3e-12 M,-11.523,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,dot_blot,,,undiluted wastewater,,DNA,dimeric,36926840,10.1021/acssensors.2c02655,"DSA1N5 also demonstrated high binding affinity in undiluted wastewater samples ( K d = 3.0 -3.9 pM for WTPV, Figure S1A,B).",step2c_acs_v1
208,SW480 cells,cell/EV,Q16520,Apt-nanovesicle,,3.66 pM,-11.437,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,cholesterol; multivalent,32049531,10.1021/jacs.9b13782,The dissociation constant ( K d ) value of Apt-nanovesicle against SW480 cells was found to be 3.66 ± 0.34 pM (Figure 2B),step2c_literal_v3
743,SARS-CoV-2 spike protein (wild type),protein,,DSA1N5,,3.9e-12 M,-11.409,avidity_multivalent,Kd,Gold,ACS,multi_agent_verified,pending_manual_supp,,,dot_blot,,,undiluted wastewater,,DNA,dimeric,36926840,10.1021/acssensors.2c02655,"DSA1N5 also demonstrated high binding affinity in undiluted wastewater samples ( K d = 3.0 -3.9 pM for WTPV, Figure S1A,B).",step2c_acs_v1
404,SARS-CoV-2 pseudotyped lentivirus (omicron variant),protein,,DSA1N5,,4.8e-12 M,-11.319,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,dot_blot,,,deionized water,,DNA,dimeric,36926840,10.1021/acssensors.2c02655,"This study demonstrates that DSA1N5 has high affinity for recognizing OMPV with a K d value of 4.8 pM, which is in the same order of magnitude as that measured for the WTPV (2.1 pM) in deionized water (DI water)",step2c_acs_v1
405,SARS-CoV-2 pseudotyped lentivirus (omicron variant),protein,,DSA1N5,,5.1e-12 M,-11.292,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,dot_blot,,,wastewater (diluted 50% with binding buffer),,DNA,dimeric,36926840,10.1021/acssensors.2c02655,DSA1N5 preserves its binding affinity in 50% wastewater ( K d = 2.1 -4.1 pM for WTPV and 5.1 for OMPV in wastewater).,step2c_acs_v1
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
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
351,thrombin,protein,P00734,Supra-TBA15/29-GO,,1.9e-11 M,-10.721,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,,,,,,DNA,Graphene Oxide immobilization; poly(adenine) anchor,31157200,10.3389/fchem.2019.00280,"Supra-TBA15 / 29-GO prepared with GO (40 μ g mL -1 ) at 60 ◦ C exhibited much higher binding affinity toward thrombin ( K d = 1.9 × 10 -11 M, Figure S10 , Supporting Information).",step2c_acs_v1
209,SW480 cells,cell/EV,Q16520,Fixed Apt-nanovesicle,,28.06 pM,-10.552,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,cholesterol; crosslinked,32049531,10.1021/jacs.9b13782,the K d value of fi xed Apt-nanovesicles to SW480 cells was increased to 28.06 ± 3.31 pM (Figure 2D),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
219,CCRF-CEM cells,cell/EV,Q9NRR3,CDN-sgc8,,0.08 nM,-10.097,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,fluorescence,,,"1 × PBS, 5 mM MgCl2",5.0,DNA,biotinylated,35670775,10.1021/acs.analchem.2c01359,Kd=0.08±0.01 nM,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
218,CCRF-CEM cells,cell/EV,Q9NRR3,mono-CDN-sgc8,,0.48 nM,-9.319,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,fluorescence,,,"1 × PBS, 5 mM MgCl2",5.0,DNA,biotinylated,35670775,10.1021/acs.analchem.2c01359,Kd= 0.48 ± 0.04 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
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
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
217,CCRF-CEM cells,cell/EV,Q9NRR3,individual sgc8,,0.82 nM,-9.086,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,fluorescence,,,"1 × PBS, 5 mM MgCl2",5.0,DNA,biotinylated,35670775,10.1021/acs.analchem.2c01359,Kd=0.82 ± 0.12 nM,step2c_literal_v3
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
228,CD8,protein,P01732,A3t,,2.0 nM,-8.699,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,,36149728,10.1021/acsami.2c11783,"A3t, a CD8 receptor-binding aptamer, which binds CD8-expressing cells with an equilibrium dissociation constant K D of 2 nM.",step2c_literal_v3
232,CD8,protein,P01732,rvCD8apt,,2.0 nM,-8.699,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,8 nt toehold,36149728,10.1021/acsami.2c11783,apparent K D = 2 nM for CD8 + cells,step2c_literal_v3
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
211,K562,protein,Q8WUY8,PAM,,3.2 nM,-8.495,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,,,,,,DNA,FAM,32307868,10.1002/anie.202004206,the K d value (3.2 nM) of PAM in binding the K562 cell is one order of magnitude lower than that of the aptamer alone (41 nM).,step2c_literal_v3
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
465,SARS-CoV-2 spike RBD,protein,,Aptx2-L,,4.900000000000001e-09 M,-8.31,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,flow_cytometry,298.15,7.4,"PBS, pH 7.4, 0.55 mM MgCl2",,DNA,,41498844,10.1021/acsami.5c16490,The Aptx2-L variant showed superior affinity with a dissociation constant ( K d) of 4.9 nM,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