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
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
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
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
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
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
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
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
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
143,P-selectin,protein,Q14242,PF377,,14.0 pM,-10.854,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377 | 14,step2c_literal_v3
147,P-selectin,protein,Q14242,PF377sl,,14.0 pM,-10.854,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,296.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377sl | 14,step2c_literal_v3
142,P-selectin,protein,Q14242,PF377,,16.0 pM,-10.796,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377 | 16,step2c_literal_v3
144,P-selectin,protein,Q14242,PF377,,18.0 pM,-10.745,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,277.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377 | 18,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
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
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
146,P-selectin,protein,Q14242,PF377sl,,29.0 pM,-10.538,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377sl | 29,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
145,P-selectin,protein,Q14242,PF377sl,,46.0 pM,-10.337,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377sl | 46,step2c_literal_v3
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
148,P-selectin,protein,Q14242,PF373sl,,56.0 pM,-10.252,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF373sl | 56,step2c_literal_v3
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
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
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
152,PDGF-BB,protein,P01127,PDGF-B aptamer,,0.1 nM,-10.0,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,,,,,DNA,2'-fluoro; 2'-O-methyl; hexaethylene glycol spacer; inverted 3'-3' thymidine cap; 40-kd PEG conjugated,9916931,10.1016/S0002-9440(10)65263-7,the binding affinity of the aptamer used in the experiments described below ( K d ≈ 0.1 nM),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
149,P-selectin,protein,Q14242,PF398sl,,178.0 pM,-9.75,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,310.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF398sl | 178,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
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
307,P-selectin,protein,Q14242,PF377sl,,250.0 pM,-9.602,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,flow_cytometry,296.15,7.4,SHMCK buffer,1.0,2'F-RNA,,9743465,10.1089/oli.1.1998.8.265,PF377sl | 250,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