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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
378,dT70,protein,,DCC-SSB,,3.0000000000000004e-09 M,-8.523,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_figure,,,,,,,,,,34085169,10.1007/s12010-021-03585-x,"At a low concentration ( ∼ 2.5 nM), the titration with dT70 gave an approximate assessment of affinity ( K d ∼ 3 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
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
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
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
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
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
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
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
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
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
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