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
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
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
319,VEGF165,protein,P15692,3R02 Bivalent,TGTGGGGGTGGACTGGGTGGGTACCTTTTTTTTTTTGTGGGGGTGGACTGGGTGGGTACC,3e-11 M,-10.523,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,23237717,10.1021/ac303023d,The K d value of 30 pM for 3R02 Bivalent was calculated by measuring SPR.,step2c_acs_v1
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
312,thrombin,protein,P00734,MP-TBA15/TBA29-T15,GGTTGGTGTGGTTGG,5.2e-11 M,-10.284,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,backfill_text_verified,,saturation_binding,,7.4,"physiological buffer (25 mM Tris-HCl (pH 7.4), 150 mM NaCl, 5.0 mM KCl, 1.0 mM MgCl2, 1.0 mM CaCl2) containing BSA (100 μM)",,DNA,thiolated; 15-mer thymidine linker,22300379,10.1021/la204651t,"MP-TBA15/TBA29-T15 -Au NPs provided high flexibility and an appropriate orientation and distance between TBA and TBA units for bivalent binding, allowing stronger interactions with thrombin ( K d = 5.2 × 10 -11 M; Supporting Information, Figure S3)",step2c_acs_v1
9,sLe X -BSA,glycan/conjugate,Q9NSU2,Clone 5,GGUGCAGGUCACUUCGAUGAGUGUAAAGCACAGGUAAGUGUCUUGGUAGAAUCGGAGUCGGUGACCGUU,5.7e-11 M,-10.244,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,KEEP_seq_in_figure,SPR,298.15,7.4,"RNA binding buffer [150 mM NaCl, 20 mM Hepes (pH 7.4), 1 mM CaCl2, 1 mM MgCl2]",1.0,RNA,,11178986,10.1006/bbrc.2001.4327,sLe X -BSA | 6.4 3 10 7 | 3.7 3 10 2 3 | 1.7 3 10 10 | 5.7 3 10 2 11,step2c_literal_v3
3,sLe X -BSA,glycan/conjugate,Q9NSU2,Clone 5,GGUGCAGGUCACUUCGAUGAGUGUAAAGCACAGGUAAGUGUCUUGGUAGAAUCGGAGUCGGUGACCGUU,8.5e-11 M,-10.071,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,KEEP_seq_in_figure,SPR,298.15,7.4,"RNA binding buffer [150 mM NaCl, 20 mM Hepes (pH 7.4), 1 mM CaCl2, 1 mM MgCl2]",1.0,RNA,,11178986,10.1006/bbrc.2001.4327,Clone 5 | 1.3 3 10 5 | 1.1 3 10 2 5 | 1.1 3 10 10 | 8.5 3 10 2 11,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
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
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
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
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
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
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
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
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
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
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
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
177,human α-thrombin,protein,P00734,5'-TMR-Apt15-T30,GGTTGGTGTGGTTGG,0.7 nM,-9.155,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 (30 T) at 3'-end,28763192,10.1021/acs.analchem.7b02313,0.7 nM for 5 ′ -TMR-Apt15-T30,step2c_literal_v3
178,human α-thrombin,protein,P00734,5'-TMR-Apt15-T35,GGTTGGTGTGGTTGG,0.7 nM,-9.155,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 (35 T) at 3'-end,28763192,10.1021/acs.analchem.7b02313,0.7 nM for 5 ′ -TMR-Apt15-T35,step2c_literal_v3
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
241,MPO,protein,P05164,MPO-14,ATATAGTACAGTGAGTAGTTGTACCACATTGTAGGTACTTAGTTGGAATG,897.0 pM,-9.047,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-14 ... K d : 897 pM,step2c_literal_v3
235,MPO,protein,P05164,MPO-03,TTCTTTGTACTACGTATGTGTTACACATCTTAAGTCCGTTTTGATGCAGC,912.0 pM,-9.04,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-03 ... 912,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
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
372,beta-conglutin,protein,,11-mer,GGTGGGGGTGG,1.05e-09 M,-8.979,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,MST,298.15,,binding buffer with 0.05% v/v Tween-20,,DNA,,33498970,10.3390/ijms22031150,KD values determined (Figure 6b) are very similar (11-mer: 1.05 nM,step2c_acs_v1
340,AP65,protein,Q13882,AP65_A1,AGCTCCAGAAGATAAATTACAGGTGAGGGCGGGCGGGTGGTTGTAATATGATCGAATGGTATATGTGTGTTTGCAACTAGGATACTATGACCCCG,1.057e-09 M,-8.976,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,ELAA,298.15,6.4,"binding buffer (10 mM phosphate, 138 mM NaCl, 2.7 mM KCl, 1.5 mM MgCl2 at pH 6.4)",,DNA,5'-biotinylated,29972299,10.1021/acsinfecdis.8b00065,A K D value of 1.057 nM was obtained using the sigmoidal dose-response curve model,step2c_acs_v1
233,MPO,protein,P05164,MPO-01,CACTCGTGAAGATCTTTAATAGATAGAATAATCGAGGTTGATTCGATGTA,1148.0 pM,-8.94,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-01 ... 1,148",step2c_literal_v3
356,HBeAg,protein,,A-9S,ACTTTTTTGGTCAGATGAGGCCTGGTGATCGTGCCCAGGCCATATGAGCAAGGAACCCCTATGCGTGCT,1.2e-09 M,-8.921,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,/5AmMC6/,32250595,10.1021/acs.analchem.9b05740,The measured dissociation constant ( K d) is improved by 19 times  from a K d value of 22.9 nM with the 80-nt sequence to a K d of 1.2 nM with the new 61-nt aptamer.,step2c_acs_v1
433,PvTRAg,protein,,Apt_16,TTAATAACATGAGTTATTGAATTATTGTTTATTTTTTTTTTTTTG,1.2e-09 M,-8.921,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,DNA,,40042916,10.1021/acsinfecdis.4c01047,"The K D of Apt_14 and Apt_16 was found to be comparable, 1.9 and 1.2 nM, respectively",step2c_acs_v1
39,prothrombin,protein,P00734,RNAR9D-14T,GGCGGUCGAUCACACAGUUCAAACGUAAUAAGCCAAUGUACGAGGCAGACGACUCGCC,1.4 nM,-8.854,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,7.4,Hepes-saline buffer,,2'F-RNA,2' Fluorocytosine; 2' Fluorouracil,22385910,10.1111/j.1538-7836.2012.04679.x,"Compared with ARC-183, RNAR9D-14T has a >40-fold higher affinity for prothrombin ( K D RNAR9D-14T = 1.4 nM",step2c_literal_v3
350,alkaline phosphatase,protein,P09923,ALP binding aptamer,CTTCTGCCCGCCTCCTTCCTGGAGGACTGTGGAGGACTTAGCGCCCATCCTTGCCCATGGAGACGAGATAGGCGGACACTC,1.49e-09 M,-8.827,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,PISA,,9.5,50 mM glycine-NaOH buffer (pH 9.5),,DNA,3'-thiol,30827094,10.1021/acs.analchem.9b00465,"Similarly, from the response -dose curve (Figure 3B), the K d value for the aptamer -MIP hybrid-coated array was estimated to be 1.49 × 10 -9 M",step2c_acs_v1
742,alkaline phosphatase,protein,P09923,ALP binding aptamer,CTTCTGCCCGCCTCCTTCCTGGAGGACTGTGGAGGACTTAGCGCCCATCCTTGCCCATGGAGACGAGATAGGCGGACACTC,1.5000000000000002e-09 M,-8.824,avidity_multivalent,Kd,Gold,ACS,multi_agent_verified,verified_in_text_or_SI,original,,PISA,,,,,DNA,3'-thiol,30827094,10.1021/acs.analchem.9b00465,giving cross-reactivity of 3.2 -5.6% and a dissociation constant of 1.5 nM,step2c_acs_v1