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
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
328,ATP,protein,P00846,Huizenga-Szostak ATP aptamer,,1.3e-09 M,-8.886,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_supp_oa,,,fluorescence,,,,,DNA,,25170558,10.1021/bc500286r,binding a ffi nity can be tuned over 4 orders of magnitude (1.3 nM -203 μ M),step2c_acs_v1
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
431,Sc3+,protein,Q96PL5,Sc-1,CTCTCGACGACGGACCATTCCCGTGGAATGACTACGTATATGTCGTC,1.0300000000000001e-08 M,-7.987,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,fluorescence,,,SELEX buffer,,DNA,,39743479,10.1021/jacs.4c13768,an apparent K d value of 10.3 nM was obtained,step2c_acs_v1
476,Escherichia coli O157:H7,protein,,E. coli O157:H7-specific aptamer,CCGGACGCTTATGCCTTGCCATCTACAGAGCAGGTGTGACGG,1.4400000000000002e-08 M,-7.842,apparent_cellular,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,fluorescence,298.15,,15% (v/v) PEG200,,DNA,FAM,41850902,10.1021/acs.analchem.5c07364,"the aptamer exhibited enhanced binding affinity in the crowded microenvironment, with a 25% reduction in Kd (from 19.2 to 14.4 nM).",step2c_acs_v1
475,Escherichia coli O157:H7,protein,,E. coli O157:H7-specific aptamer,CCGGACGCTTATGCCTTGCCATCTACAGAGCAGGTGTGACGG,1.92e-08 M,-7.717,apparent_cellular,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,fluorescence,298.15,,liquid milk-based matrices (0% lactalbumin/lactose/casein),,DNA,FAM,41850902,10.1021/acs.analchem.5c07364,"the aptamer exhibited enhanced binding affinity in the crowded microenvironment, with a 25% reduction in Kd (from 19.2 to 14.4 nM).",step2c_acs_v1
424,verrucarin A,protein,,Ver1_JYP,,2.9500000000000003e-08 M,-7.53,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,,7.4,SELEX buffer,,DNA,,39404132,10.1021/acs.analchem.4c03307,The novel ssDNA aptamer exhibited a binding affinity of 29.5 nM,step2c_acs_v1
354,paramylon,protein,,Par-15,,3.49e-08 M,-7.457,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,,7.5,"binding buffer (50 mM Tris, 150 mM NaCl, 5 mM MgCl2, 1 mM EDTA, pH 7.5)",,DNA,FAM,31809034,10.1021/acs.jafc.9b04588,"The estimated K d values of fi ve selected aptamers, Par-7, Par-15, Par-18, Par-20, and Par-22, are 17.45 ± 2.61, 34.90 ± 5.83, 64.06 ± 6.72, 123.81 ± 13.41, and 249.52 ± 46.39 nM, respectively.",step2c_acs_v1
355,paramylon,protein,,Par-18,,6.406e-08 M,-7.193,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,,7.5,"binding buffer (50 mM Tris, 150 mM NaCl, 5 mM MgCl2, 1 mM EDTA, pH 7.5)",,DNA,FAM,31809034,10.1021/acs.jafc.9b04588,"The estimated K d values of fi ve selected aptamers, Par-7, Par-15, Par-18, Par-20, and Par-22, are 17.45 ± 2.61, 34.90 ± 5.83, 64.06 ± 6.72, 123.81 ± 13.41, and 249.52 ± 46.39 nM, respectively.",step2c_acs_v1
135,SCAF4,protein,O95104,PTf-SRiApt,TTAAAGGGGTGGGGAGTCAT,0.073 µM,-7.137,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,6.5,"30 mM MES buffer pH 6.5, 25 mm NaCl, 2 mm β-ME, 1 mm CHAPS, and 0.002 mg mL -1 BSA",,DNA,phosphorothioate,40574704,10.1002/advs.202500433,0.073 ± 0.003 µ m for PTf -SRiApt,step2c_literal_v3
52,hemagglutinin (HA) protein of H1N1 influenza virus (A/Puerto Rico/8/1934),protein,,aptamer 1,GGGAGCTCAGAATAAACGCTCAAGGCACGGCATGTGTGGTATGTGGTGCCTGTACTCGTTCGACATGAGGCCCGGATC,78.0 nM,-7.108,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,310.15,7.35,"binding buffer (20 mM HEPES buffer pH 7.35, 120 mM NaCl, 1 mM MgCl2, 1 mM CaCl2, and 5 mM KCl)",1.0,DNA,,26904922,10.1089/nat.2015.0564,"As it showed a higher binding affinity for HA protein (Kd = 78 -1nM), aptamer 1 was tested",step2c_literal_v3
400,6'-sialyllactose,protein,Q9Y3R4,Apt9-1,,9.175000000000001e-08 M,-7.037,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,298.15,7.4,10 mM PBS (pH 7.4),,DNA,,36700646,10.1021/acs.jafc.2c07784,A 35 nt truncated aptamer Apt9-1 ( K d = 91.75 nM) with higher affinity than Apt9 was finally obtained.,step2c_acs_v1
102,CD9,protein,P21926,CD9-26,ATAGTCCCTTGGCGTGCTTCACAACCTTGAACTTGACGCAGGATCGTTCAGTGCGCACTAGAGCAGGTACGGTGTCA,101.96 nM,-6.992,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,277.15,,1 × SELEX buffer,,DNA,,37585601,10.1021/acssensors.3c00879,CD9-26 | 5 ′ -ATA GTC CCT TGG CGT GCT TCA CAA CCT TGA ACT TGA CGC AGG ATC GTT CAG TGC GCA CTA GAG CAG GTA CGG TGT CA-3 ′ | - 8.92,step2c_literal_v3
474,Moraxella osloensis,protein,,MO9,GCATTCAGAGCCATCCACCCTGAAGGTGGCGTATATCGATGTTCGGGACGCCGTGCCTGTTGCGTACGAATGG,1.1890000000000001e-07 M,-6.925,apparent_cellular,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,fluorescence,,,,,DNA,thiolated,41784024,10.1021/acssensors.5c03424,high-a ffi nity aptamer (K d = 118.9 nM),step2c_acs_v1
134,SCAF4,protein,O95104,PT1/2-SRiApt,TTAAAGGGGTGGGGAGTCAT,0.121 µM,-6.917,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,6.5,"30 mM MES buffer pH 6.5, 25 mm NaCl, 2 mm β-ME, 1 mm CHAPS, and 0.002 mg mL -1 BSA",,DNA,phosphorothioate,40574704,10.1002/advs.202500433,0.121 ± 0.054 µ m for PT1/2 -SRiApt,step2c_literal_v3
436,SIRT2,protein,Q8IXJ6,Apt 45,,1.233e-07 M,-6.909,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,310.15,,,,DNA,FAM,40200675,10.1021/acs.analchem.5c00066,selected Apt 45 ( K d = 123.3 nM) to fabricate the 'turn-on' fluorescent biosensor,step2c_acs_v1
399,6'-sialyllactose,protein,Q9Y3R4,Apt9,,1.5230000000000003e-07 M,-6.817,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,298.15,7.4,10 mM PBS (pH 7.4),,DNA,,36700646,10.1021/acs.jafc.2c07784,The ssDNA aptamer Apt9 ( K d = 152.3 nM) with a length of 79 nucleotides (nt) was demonstrated as the optimal aptamer candidate,step2c_acs_v1
133,SCAF4,protein,O95104,PT1/3-SRiApt,TTAAAGGGGTGGGGAGTCAT,0.223 µM,-6.652,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,6.5,"30 mM MES buffer pH 6.5, 25 mm NaCl, 2 mm β-ME, 1 mm CHAPS, and 0.002 mg mL -1 BSA",,DNA,phosphorothioate,40574704,10.1002/advs.202500433,0.223 ± 0.030 µ m for PT 1/3 -SRiApt,step2c_literal_v3
467,benzovindiflupyr,protein,,Apt.BZF01,,2.2650000000000002e-07 M,-6.645,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,,,,,DNA,,41614999,10.1021/acs.jafc.5c15044,corrected KDs of 226.5 nM (Apt.BZF01),step2c_acs_v1
103,CD9,protein,P21926,CD9-28,ATAGTCCCTTGGCGTGCTTCACAACCTTGAACTTGACGCAGGATCGTTCAGGGCGCACTAGAGCAGGTACGGTGTCA,289.67 nM,-6.538,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,277.15,,1 × SELEX buffer,,DNA,,37585601,10.1021/acssensors.3c00879,CD9-28 | 5 ′ -ATA GTC CCT TGG CGT GCT TCA CAA CCT TGA ACT TGA CGC AGG ATC GTT CAG GGC GCA CTA GAG CAG GTA CGG TGT CA-3 ′ | - 8.80,step2c_literal_v3
450,biliverdin,protein,P53004,Bvd4,GACGACGGGTGTGGAACAGTGCGAATACTTTCGAGTCGTC,4.0999999999999994e-07 M,-6.387,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,fluorescence,,7.6,selection buffer,,DNA,,40669049,10.1021/acschembio.5c00438,"Titration of biliverdin into 1 μM Bvd4 aptamer led to an approximate 90% fluorescence drop (Figure 3A), and the fitted dissociation constant ( K d ) was 0.41 μM",step2c_acs_v1
132,SCAF4,protein,O95104,SRiApt,TTAAAGGGGTGGGGAGTCAT,0.469 µM,-6.329,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,6.5,"30 mM MES buffer pH 6.5, 25 mm NaCl, 2 mm β-ME, 1 mm CHAPS, and 0.002 mg mL -1 BSA",,DNA,,40574704,10.1002/advs.202500433,The binding affinities (K D ) were determined to be 0.469 ± 0.010 µ m for unmodified SRiApt,step2c_literal_v3
246,CD9,protein,P21926,CD9-08,TGACACCGTACCTGCTCTAGTGCGCACTGAACGATCCTGCGTCAAGTTCAAGGTTGTGAAGCACGCCAAGGGACTAT,494.37 nM,-6.306,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,277.15,,1 × SELEX buffer,,DNA,,37585601,10.1021/acssensors.3c00879,CD9-08 | 5 ′ -TGA CAC CGT ACC TGC TCT AGT GCG CAC TGA ACG ATC CTG CGT CAA GTT CAA GGT TGT GAA GCA CGC CAA GGG ACT AT-3 ′ | - 11.71,step2c_literal_v3
453,bilirubin,protein,P22309,Brb7,GACGACATAAGCTCTTAGCGCGTGTTTACCACCTTTGTCGTC,1.4e-06 M,-5.854,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,fluorescence,,7.6,selection buffer,,DNA,,40669049,10.1021/acschembio.5c00438,"After titrating bilirubin into 1.0 μM Brb7 aptamer, the saturation fluorescence decrease reached 99% (Figure 6A) and its K d was fitted to be 1.4 μM",step2c_acs_v1
451,biliverdin,protein,P53004,Bvd1,GACGACGAACGGAGTAGGTTTTAACGAATGAAATGGGTCGTC,2e-06 M,-5.699,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,fluorescence,,7.6,selection buffer,,DNA,,40669049,10.1021/acschembio.5c00438,"The same trend was also observed for the Bvd1 aptamer (Figure S1), and the fitted K d was 2.0 μM.",step2c_acs_v1
425,verrucarin A,protein,,14_Ver1,,2.2e-06 M,-5.658,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,,7.4,SELEX buffer,,DNA,6-FAM at 5'-end; dabcyl at 3'-end,39404132,10.1021/acs.analchem.4c03307,The binding test demonstrated that the decrease in fluorescence was correlated with increasing verrucarin A concentration with K D = 2.2 μM.,step2c_acs_v1
426,verrucarin A,protein,,Ver1_JYP (C32G mutant),,2.2999999999999996e-06 M,-5.638,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,,7.4,SELEX buffer,,DNA,C32G mutation,39404132,10.1021/acs.analchem.4c03307,guanine with both functional groups exhibited partially recovered binding activity ( K D = 2.3 μM).,step2c_acs_v1
122,hemin,protein,Q9NP58,Sequence D,GGTTGGTGTGGTTGG,2.9 μM,-5.538,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,7.4,"10 mM K-phosphate, pH 7.4, 0.1 M KCl, and 1% DMSO",,DNA,"phosphorothioate (Sp, stereopure)",40368877,10.1021/acs.molpharmaceut.5c00117,"Fitting to a one-site specific binding model using GraphPad Prism software yields the dissociation constant of 8.3 and 2.9 μ M for sequences C and D, respectively.",step2c_literal_v3
123,hemin,protein,Q9NP58,Sequence C,GGTTGGTGTGGTTGG,8.3 μM,-5.081,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,fluorescence,,7.4,"10 mM K-phosphate, pH 7.4, 0.1 M KCl, and 1% DMSO",,DNA,"phosphorothioate (Rp, stereopure)",40368877,10.1021/acs.molpharmaceut.5c00117,"Fitting to a one-site specific binding model using GraphPad Prism software yields the dissociation constant of 8.3 and 2.9 μ M for sequences C and D, respectively.",step2c_literal_v3
454,bilirubin,protein,P22309,Brb9,GACGACGAATGCAATGGGGCCTGCCGAACGTCTTTAGGATTT,9e-06 M,-5.046,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,fluorescence,,7.6,selection buffer,,DNA,,40669049,10.1021/acschembio.5c00438,"The same trend was also observed in the Brb9 aptamer (Figure S4), which showed a K d of 9.0 μM.",step2c_acs_v1
463,Patulin,protein,,PTL-1,,1.8399999999999997e-05 M,-4.735,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,,6.0,"selection buffer (10 mM MES, pH 6.0, 150 mM NaCl, 5 mM MgCl2)",,DNA,,41473783,10.1186/s44280-025-00101-2,yielding an apparent K d of 18.4 μM,step2c_acs_v1
124,dehydroepiandrosterone sulfate,protein,Q06520,"DHEAS aptamer (stem, Rp)",,32.03 μM,-4.494,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,fluorescence,,8.0,"20 mM Tris Buffer, 1 M NaCl, 10 mM MgCl2, pH 8.0",10.0,DNA,"phosphorothioate (Rp, stereopure); fluorescein",40368877,10.1021/acs.molpharmaceut.5c00117,Values calculated are 32.03 μ M for stem Rp,step2c_literal_v3
126,dehydroepiandrosterone sulfate,protein,Q06520,"DHEAS aptamer (loop, Rp)",,33.28 μM,-4.478,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,fluorescence,,8.0,"20 mM Tris Buffer, 1 M NaCl, 10 mM MgCl2, pH 8.0",10.0,DNA,"phosphorothioate (Rp, stereopure); fluorescein",40368877,10.1021/acs.molpharmaceut.5c00117,33.28 μ M for loop Rp,step2c_literal_v3
125,dehydroepiandrosterone sulfate,protein,Q06520,"DHEAS aptamer (stem, Sp)",,36.57 μM,-4.437,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,fluorescence,,8.0,"20 mM Tris Buffer, 1 M NaCl, 10 mM MgCl2, pH 8.0",10.0,DNA,"phosphorothioate (Sp, stereopure); fluorescein",40368877,10.1021/acs.molpharmaceut.5c00117,36.57 μ M for stem Sp,step2c_literal_v3
464,Patulin,protein,,PAT-6,,4.8e-05 M,-4.319,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,,6.0,"20 mM MES buffer, pH = 6.0, with 150 mM NaCl and 2.0 mM MgCl2",,DNA,,41473783,10.1186/s44280-025-00101-2,"PAT-6 has weaker binding affinities ( Kd = 48 μM by ThT, Fig. 4S)",step2c_acs_v1
127,dehydroepiandrosterone sulfate,protein,Q06520,"DHEAS aptamer (loop, Sp)",,59.62 μM,-4.225,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,fluorescence,,8.0,"20 mM Tris Buffer, 1 M NaCl, 10 mM MgCl2, pH 8.0",10.0,DNA,"phosphorothioate (Sp, stereopure); fluorescein",40368877,10.1021/acs.molpharmaceut.5c00117,59.62 μ M for loop Sp,step2c_literal_v3
468,L-lactate,protein,Q9BYZ2,D-Lac1103,TGATGTCGTC,8.999999999999999e-05 M,-4.046,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,backfill_text_verified,,fluorescence,,,,,DNA,FAM,41779931,10.1021/acs.analchem.5c07149,The true K d for D-Lac1103 was calculated to be 0.09 mM for L-lactate,step2c_acs_v1
471,L-lactate,protein,Q9BYZ2,Lac201,,0.0009000000000000001 M,-3.046,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,296.15,,SELEX buffer,,DNA,2AP,41779931,10.1021/acs.analchem.5c07149,"the fitted K d was 0.9 mM (Figure 5C, black line)",step2c_acs_v1
469,D-lactate,protein,Q86WU2,D-Lac1103,TGATGTCGTC,0.0025 M,-2.602,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,backfill_text_verified,,fluorescence,295.15,,SELEX buffer,,DNA,FAM,41779931,10.1021/acs.analchem.5c07149,"In addition, the apparent K d values for D-Lac1103 are 0.46 mMfor L-lactate and 2.5 mM for D-lactate",step2c_acs_v1
457,Tris(hydroxymethyl)aminomethane,protein,,Tris aptamer,,0.0026000000000000003 M,-2.585,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,,,,,DNA,,40905906,10.1021/acs.analchem.5c03351,ThT yielded K d values changed modestly from 1.6 to 2.6 mM,step2c_acs_v1
473,L-lactate,protein,Q9BYZ2,Lac2059,,0.0033 M,-2.481,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,296.15,,SELEX buffer,,DNA,2AP,41779931,10.1021/acs.analchem.5c07149,The fitted K d was 3.3 mM for this 2AP-labeled aptamer,step2c_acs_v1
472,L-lactate,protein,Q9BYZ2,Lac201,,0.0043 M,-2.367,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,fluorescence,296.15,,SELEX buffer,,DNA,2AP,41779931,10.1021/acs.analchem.5c07149,although the obtained K d (4.3 mM) was about 5-fold higher than that obtained using Mg 2+ .,step2c_acs_v1
438,acrylamide,protein,P41145,AA-1,GACGACGGAATCCTGGTGCACGTTGGTGGAGGTCACGTCGTC,0.0047 M,-2.328,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,fluorescence,,7.4,20 mM HEPES buffer (pH 7.4) with 100 mM NaCl and 1 mM MgCl2,,DNA,,40261307,10.1021/acs.analchem.5c00783,"Similarly, the AA-1 aptamer exhibited a true K d value of 4.7 mM via the strand-displacement assay",step2c_acs_v1
437,acrylamide,protein,P41145,AA-1,GACGACGGAATCCTGGTGCACGTTGGTGGAGGTCACGTCGTC,0.0105 M,-1.979,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,fluorescence,,7.4,"20 mM HEPES pH 7.4, 100 mM NaCl, and 1 mM MgCl2",,DNA,,40261307,10.1021/acs.analchem.5c00783,the fitted K d value was 10.5 mM,step2c_acs_v1