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
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
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
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
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
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
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
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
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
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
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
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
394,IgE,protein,P0DOX4,S2,GACTACCCGGGTATCTAATCCGACCATTTTTCGTCTCCTTTGTACGAGCAGTGTGCTCGACCTGCCGCCCGTAGG,1.5500000000000002e-09 M,-8.81,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,NECEEM,,9.0,10 mM Tris-HCl buffer (pH 9.0),,DNA,FITC,36144553,10.3390/molecules27185818,"Based on the results of these experiments, the K D values of S1 and S2 were estimated to be 0.83 and 1.55 nM, respectively",step2c_acs_v1
359,HBeAg,protein,,EAg3,TTTTTTTTGGGCGAAGACCGGGACGGGAGGAAAGAGATGTTTGGTTTT,1.7000000000000001e-09 M,-8.77,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,,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, as compared to the K d value of 1.7 nM with the unmodi fi ed EAg3 aptamer.",step2c_acs_v1
374,beta-conglutin,protein,,TT-11-mer,TTGGTGGGGGTGG,1.88e-09 M,-8.726,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 (... TT-11 mer: 1.88 nM,step2c_acs_v1
376,beta-conglutin,protein,,11-mer-TT,GGTGGGGGTGGTT,2.59e-09 M,-8.587,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 (... and 11-mer-TT: 2.59 nM),step2c_acs_v1
375,beta-conglutin,protein,,TT-11-mer-TT,TTGGTGGGGGTGGTT,2.71e-09 M,-8.567,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 (... TT-11-mer-TT: 2.71 nM,step2c_acs_v1
367,SARS-CoV-2 RBD,protein,,CoV2-RBD-1,CAGCACCGACCTTGTGCTTTGGGAGTGCTGGTCCAAGGGCGTTAATGGACA,3.1000000000000005e-09 M,-8.509,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,backfill_text_verified,,flow_cytometry,,,PBS with 0.55 mM MgCl2,,DNA,,32551560,10.1021/acs.analchem.0c01394,the dissociation constant values ( K d) of the CoV2-RBD-1 aptamer ... were 3.1 nM,step2c_acs_v1
410,melamine,protein,,Apt M,TTCCTTTTCTCTCC,4.4000000000000005e-09 M,-8.357,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,backfill_text_verified,,,,,,,DNA,abasic site,37343019,10.1021/acs.analchem.2c05777,dissociation constant K d = 4.4 nM,step2c_acs_v1
320,VEGF165,protein,P15692,VEap121,TGTGGGGGTGGACGGGCCGGGTAGA,4.700000000000001e-09 M,-8.328,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,SPR,293.15,7.4,"Tris-buffered saline (TBS: 10 mM Tris-HCl, 100 mM NaCl, 5 mM KCl, pH 7.4)",,DNA,,23237717,10.1021/ac303023d,As the calculated K d value of VEap121 was 4.7 nM,step2c_acs_v1
327,Myoglobin,protein,P02144,Myo40-7-27,CCCTCCTTTCCTTCGACTAGATCTGCTGCGTTGTTCCGA,4.93e-09 M,-8.307,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,DNA,,24914856,10.1021/ac501088q,The aptamer with the highest a ffi nity ( K d = 4.93 nM) was then used for the fabrication of a label-free supersandwich electrochemical biosensor for Myo detection,step2c_acs_v1
455,biliverdin,protein,P53004,Bvd4,GACGACGGGTGTGGAACAGTGCGAATACTTTCGAGTCGTC,6.000000000000001e-09 M,-8.222,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,40669049,10.1021/acschembio.5c00438,"For the biliverdin selection, the tightest affinity aptamer has a dissociation costant ( K d ) value of 6 nM determined using isothermal titration calorimetry (ITC)",step2c_acs_v1
313,Salmonella enteritidis,protein,P29460,SENT-9,CTCCTCTGACTGTAACCACGCACAAAGGCTCGCGCATGGTGTGTACGTTCTTACAGAGGT,7.000000000000001e-09 M,-8.155,apparent_cellular,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,22971146,10.1021/ac302217u,It was observed that the aptamer pool collected at the seventh round of selection had the highest binding a ffi nity to the bacteria ( K D = 7 nM).,step2c_acs_v1
445,Cu2+,protein,Q6UVY6,Co-1,GACGACGGAACGGAGGTTCTTAGGTCGGTAGACCGAGTCGTC,8e-09 M,-8.097,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,40656531,10.1039/d5sc02436f,The corresponding true K d values were ... 8 nM for Cu 2+,step2c_acs_v1
309,Streptococcus pyogenes M-type mixture,protein,,20A24P,AAGCAGCACAGAGGTCAGATGGGGGGAAGACACAGAGAAAGGCCGGGGTGAAGTGTAGAGGCCTATGCGTGCTACCGTGAA,9.000000000000001e-09 M,-8.046,apparent_cellular,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,flow_cytometry,,7.4,"binding buffer (1-BB; 50 mM Tris-HCl(pH7.4), 5 mM KCl, 100 mM NaCl, 1 mM MgCl2)",,DNA,5'-FAM,21504182,10.1021/ac200575e,"Two aptamers, 20A24P and 15A3P (with estimated binding dissociation constants of 9 and 10 nM, respectively)",step2c_acs_v1
362,HBeAg,protein,,EAg2,TTTTTTTTGGGCGAAGACCGGGACGGGAGGAAAGTGTAGATTGGAAAA,9.2e-09 M,-8.036,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,,32250595,10.1021/acs.analchem.9b05740,"A comparison of the binding of HBeAg with the four aptamers (Figure S3) shows K d values of 44.2 nM for EAg0, 9.5 nM for EAg1, 9.2 nM for EAg2",step2c_acs_v1
361,HBeAg,protein,,EAg1,TTTTTTTTGGGCGAAGACCGGGACGGGAGGAAAGTGTAGATTGGTTTT,9.5e-09 M,-8.022,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,,32250595,10.1021/acs.analchem.9b05740,"A comparison of the binding of HBeAg with the four aptamers (Figure S3) shows K d values of 44.2 nM for EAg0, 9.5 nM for EAg1",step2c_acs_v1
310,Streptococcus pyogenes M-type mixture,protein,,15A3P,ATTCACGGTAGCACGCATAGGGACAGCAAGCCCAAGCTGGGTGTGCAAGGTGAGGAGTGGG,1e-08 M,-8.0,apparent_cellular,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,flow_cytometry,,7.4,"binding buffer (1-BB; 50 mM Tris-HCl(pH7.4), 5 mM KCl, 100 mM NaCl, 1 mM MgCl2)",,DNA,5'-FAM,21504182,10.1021/ac200575e,"Two aptamers, 20A24P and 15A3P (with estimated binding dissociation constants of 9 and 10 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
427,U87MG GBM with IDH1 htz mutation,protein,,Gli-55,GTCCGGTTCAACCTCTAGCATTCCTGGCGTTATTAACGGAGCAGTCCTGTGGAGTGGGTGA,1.22e-08 M,-7.914,apparent_cellular,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,flow_cytometry,298.15,,DPBS,,DNA,Cy5,39682297,10.3390/cancers16234111,The apparent dissociation constant measured for U87MG GBM with the IDH1 htz mutation ( Kd ) of Gli-55 is 12.2 nM,step2c_acs_v1
344,PlanarAu,protein,,1N truncated,TATGCATGTGTATATCAACACTCCGGGTCTAATCGTTCA,1.304e-08 M,-7.885,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,QCM,,,AIB,,DNA,,30189130,10.1021/acscombsci.8b00048,1N truncated (Kd = 13.04 nM),step2c_acs_v1
368,SARS-CoV-2 RBD,protein,,CoV2-RBD-4,ATCCAGAGTGACGCAGCATTTCATCGGGTCCAAAAGGGGCTGCTCGGGATTGCGGATATGGACACGT,1.3600000000000001e-08 M,-7.866,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,backfill_text_verified,,flow_cytometry,,,PBS with 0.55 mM MgCl2,,DNA,,32551560,10.1021/acs.analchem.0c01394,the dissociation constant values ( K d) of the ... CoV2-RBD-4 aptamer ... were ... 13.6 nM,step2c_acs_v1
428,U87MG GBM with IDH1 htz mutation,protein,,Gli-35,GCGTTATTAACGGAGCAGTCCTGTGGAGTGGGTGA,1.3600000000000001e-08 M,-7.866,apparent_cellular,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,flow_cytometry,298.15,,DPBS,,DNA,Cy5,39682297,10.3390/cancers16234111,"while for Gli-35, it is 13.6 nM.",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
411,thrombin,protein,P00734,TBA15-AnBtz,GGTTGGTGTGGTTGGTATATT,1.5000000000000002e-08 M,-7.824,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,37857354,10.1021/acs.bioconjchem.3c00373,apparent dissociation constant ( K d ) of 15 nM,step2c_acs_v1
330,Progesterone,protein,P06401,P4G13,GCATCACACACCGATACTCACCCGCCTGATTAACATTAGCCCACCGCCCACCCCCGCTGC,1.7e-08 M,-7.77,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,25486123,10.1021/ac503639s,"The dissociation constant of the best aptamer, designated as P4G13, was estimated to be 17 nM by electrochemical impedance spectroscopy (EIS) as well as fl uorometric assay.",step2c_acs_v1
421,hnRNP A1,protein,P09651,AS1411,GGTGGTGGTGGTTGTGGTGGTGGTGG,1.75e-08 M,-7.757,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,BLI,,7.4,"BLI buffer (20 mM phosphate buffer, 8 mM KCl, 137 mM NaCl, 0.05% surfactant P20)",,DNA,,38784467,10.1039/d3md00752a,"for AS1411, the K d value was 17.5 nM (Fig. 6B)",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
441,xanthylacrylamide,protein,,XAA-1,GACGACGTAGGTGTGGATGGCTTTGAAAAAGGGCTAGTCGTC,2e-08 M,-7.699,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,40261307,10.1021/acs.analchem.5c00783,The true K d of aptamer XAA-1 was calculated to be 20 nM after accounting for the competitive effect of the quencher-labeled strand,step2c_acs_v1
422,hnRNP A1,protein,P09651,TBA,GGTTGGTGTGGTTGG,2.1100000000000004e-08 M,-7.676,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,BLI,,7.4,"BLI buffer (20 mM phosphate buffer, 8 mM KCl, 137 mM NaCl, 0.05% surfactant P20)",,DNA,,38784467,10.1039/d3md00752a,"for TBA, the K d value was 21.1 nM (Fig. 6A)",step2c_acs_v1
357,HBeAg,protein,,A-9,AGCAGCACAGAGGTCAGATGAGGCCTGGTGATCGTGCCCAGGCCATATGAGCAAGGAACCCCTATGCGTGCTACCGTGAA,2.29e-08 M,-7.64,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,,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
373,beta-conglutin,protein,,11-mer,GGTGGGGGTGG,2.3300000000000003e-08 M,-7.633,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,BLI,303.15,7.4,"PBS, 1.5 mM MgCl2, pH 7.4, 0.1% Tween-20",,DNA,,33498970,10.3390/ijms22031150,A 2:1 heterogenous model was used to fit the data and calculate the binding affinities resulting in two different KD values of 6.95 and 23.30 nM.,step2c_acs_v1
485,melamine,protein,,Mel36-1,GGAGTTCGTAGAGGTGTCCTAAGTCTTTAGGTTGGA,2.4000000000000003e-08 M,-7.62,non_intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,backfill_text_verified,,,298.15,,,,,,42261635,10.1021/acs.analchem.6c01553,Mel36-1 has the most sensitive response with an apparent K d of 24 nM,step2c_acs_v1
317,Salmonella typhimurium,protein,Q8IWE5,STYP-3,GAGTTAATCAATACAAGGCGGGAACATCCTTGGCGGTGC,2.5000000000000002e-08 M,-7.602,apparent_cellular,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,,,,,,,,23075417,10.1021/ac302902s,It was observed that the aptamer pool collected at the seventh round of selection had the highest binding a ffi nity to the bacteria ( K D = 25 nM).,step2c_acs_v1
416,Sterigmatocystin,protein,,H Seq02,GAATACGGATTACTGTTCGTACTGACCTATGCTGTGGAGT,2.53e-08 M,-7.597,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,ITC,,,,,DNA,amino-modified,38175632,10.1021/acs.analchem.3c03675,"The final fitting curve showed a reduced chi-squared (kcal/mol) 2 of 0.871, and the K D value was 25.3 nM.",step2c_acs_v1