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
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
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
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
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
55,von Willebrand factor A1-domain,protein,P04275,ARC1172-41,,326.0 pM,-9.487,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,SPR,310.15,,1 × PBS supplemented with 0.05% (w/v) Nonidet P-40,,DNA,,27966933,10.1021/jacs.6b10767,ARC1172-41 ( K D = 326 pM),step2c_literal_v3
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
247,Human thrombin,protein,P00734,Lin08-08,,0.4 nM,-9.398,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Lin(08-08) | 1.63 10^6 | 6.94 10^-4 | 0.4,step2c_literal_v3
249,Human thrombin,protein,P00734,Pse08-08,,0.4 nM,-9.398,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Pse(08-08) | 1.19 10^6 | 5.10 10^-4 | 0.4,step2c_literal_v3
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
54,von Willebrand factor A1-domain,protein,P04275,Pr-DsDsDs-40,,1.03 nM,-8.987,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,Pr-DsDsDs-40 ( K D = 1.03 nM),step2c_literal_v3
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
108,thrombin,protein,P00734,T.7,,1.5 nM,-8.824,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,SPR,,,binding buffer supplemented with 0.05% of Tween-20,,DNA,,37798416,10.1038/s41587-023-01973-8,T.7 exhibited the strongest binding signal with a 1.5 nM K d,step2c_literal_v3
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
30,thrombin,protein,P00734,HD22,AGTCCGTGGTAGGGCAGGTTGGGGTGACT,2.4e-09 M,-8.62,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,,,,,DNA,,18826387,10.1111/j.1538-7836.2008.03162.x,HD22 | Thrombin | K D ( M) | 2.4 · 10 ) 9,step2c_literal_v3
251,Human thrombin,protein,P00734,Pse08-29,TGACCTCTAGTGACTGATTTACGAGTC,2.6 nM,-8.585,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,backfill_text_verified,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Pse(08 - 29) | 1.33 10^6 | 3.47 10^-3 | 2.6,step2c_literal_v3
16,thrombin,protein,P00734,TBA,GGTTGGTGTGGTTGG,2.86e-09 M,-8.544,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,,,,,DNA,biotin at 3' end; six-carbon spacer,16053288,10.1021/ac0502450,thrombin | 2.2 10 5 | 6.3 10 - 4 | 3.4 10 8 | 2.86 10 - 9,step2c_literal_v3
156,prothrombin,protein,P00734,HD1,GGTTGGTGTGGTTGG,3.5e-09 M,-8.456,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,,,,,DNA,,18826387,10.1111/j.1538-7836.2008.03162.x,HD1 | Prothrombin+ phospholipids | K D ( M) | 3.5 · 10 ) 9,step2c_literal_v3
250,Mouse thrombin,protein,,Pse08-08,,4.2 nM,-8.377,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Pse(08-08) | 7.35 10^5 | 3.06 10^-3 | 4.2,step2c_literal_v3
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
252,Mouse thrombin,protein,,Pse08-29,TGACCTCTAGTGACTGATTTACGAGTC,6.3 nM,-8.201,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,backfill_text_verified,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Pse(08 - 29) | 6.72 10^5 | 4.26 10^-3 | 6.3,step2c_literal_v3
248,Mouse thrombin,protein,,Lin08-08,,6.7 nM,-8.174,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,Lin(08-08) | 6.41 10^5 | 4.30 10^-3 | 6.7,step2c_literal_v3
28,thrombin,protein,P00734,HD1,GGTTGGTGTGGTTGG,7.1e-09 M,-8.149,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,,,,,DNA,,18826387,10.1111/j.1538-7836.2008.03162.x,HD1 | Thrombin | K D ( M) | 7.1 · 10 ) 9,step2c_literal_v3
139,PTK7,protein,Q13308,4AsF,,7.2 nM,-8.143,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_supp,,,SPR,310.15,7.4,1 × DPBS,5.0,DNA,"SF at positions A23, A24, A25, A26",41065179,10.1021/jacs.5c11823,"4AsF, which exhibited a 10-fold reduction compared to 4APS (0.77 vs 7.20 nM)",step2c_literal_v3
194,α-thrombin,protein,P00734,TBA-iT7,GGTTGGTGTGGTTGG,9.9 nM,-8.004,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,,100 mM KCl,,DNA,3'-inverted thymidine at position 7,30735210,10.1039/c9ob00053d,TBA-iT7 | 9.9,step2c_literal_v3
17,thrombin-HRP,protein,,TBA,GGTTGGTGTGGTTGG,1.13e-08 M,-7.947,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,,,,,DNA,biotin at 3' end; six-carbon spacer,16053288,10.1021/ac0502450,thrombin-HRP | 6.7 10 4 | 7.6 10 - 4 | 8.7 10 7 | 1.13 10 - 8,step2c_literal_v3
198,α-thrombin,protein,P00734,TBA-iT9,GGTTGGTGTGGTTGG,11.5 nM,-7.939,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,,100 mM KCl,,DNA,3'-inverted thymidine at position 9,30735210,10.1039/c9ob00053d,TBA-iT9 | 11.5,step2c_literal_v3
196,α-thrombin,protein,P00734,TBA-G8-iT8,GGTTGGTTTGGTTGG,12.4 nM,-7.907,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,,100 mM KCl,,DNA,3'-inverted thymidine at position 8,30735210,10.1039/c9ob00053d,TBA-G8-iT8 | 12.4,step2c_literal_v3
14,Le A,protein,P00488,Clone 5,GGUGCAGGUCACUUCGAUGAGUGUAAAGCACAGGUAAGUGUCUUGGUAGAAUCGGAGUCGGUGACCGUU,1.4e-08 M,-7.854,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,KEEP_seq_in_figure,SPR,,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,Le A | 7.3 3 10 2 | 1.0 3 10 2 5 | 7.2 3 10 7 | 1.4 3 10 2 8,step2c_literal_v3
193,α-thrombin,protein,P00734,TBA-iT7,GGTTGGTGTGGTTGG,15.9 nM,-7.799,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,7.4,"138 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, and 1.76 mM KH2PO4, pH 7.4, 0.05% Tween-20",,DNA,3'-inverted thymidine at position 7,30735210,10.1039/c9ob00053d,TBA-iT7 | 15.9,step2c_literal_v3
314,hMMP-9,protein,,F3Bomf,,2e-08 M,-7.699,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_supp,,,SPR,296.15,,PBS buffer,,2'-OMe-RNA,2'-O-methyl purine; 2'-fluoro pyrimidine; 5'-hexylamino linker; 5'-MAG3 conjugate,23043415,10.1021/bc300146c,"The K d was taken as the concentration leading to half saturation, i.e., about 20 nM.",step2c_acs_v1
107,Mouse thrombin,protein,,TBA29,TGACCCTAGTGACTGATTTACGAGGTC,22.0 nM,-7.658,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,backfill_text_verified,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,TBA29 | 2.76 10^5 | 6.07 10^-3 | 22.0,step2c_literal_v3
13,Le X,protein,O15496,Clone 5,GGUGCAGGUCACUUCGAUGAGUGUAAAGCACAGGUAAGUGUCUUGGUAGAAUCGGAGUCGGUGACCGUU,2.4e-08 M,-7.62,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,KEEP_seq_in_figure,SPR,,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,Le X | 6.7 3 10 2 | 1.6 3 10 2 5 | 4.1 3 10 7 | 2.4 3 10 2 8,step2c_literal_v3
189,α-thrombin,protein,P00734,TBA,GGTTGGTGTGGTTGG,27.2 nM,-7.565,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,7.4,"138 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, and 1.76 mM KH2PO4, pH 7.4, 0.05% Tween-20",,DNA,,30735210,10.1039/c9ob00053d,TBA | 27.2,step2c_literal_v3
352,FGFR3 K650E,protein,,SU-3,CAGAGGCTGACGTAAACAGACATTGATGGGACCCACCCTTCCGCTGGCAA,2.82e-08 M,-7.55,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,SPR,,,1 × PBS,,DNA,,31265241,10.1021/acscombsci.9b00059,"The predicted K D was 28.2 × 10 -9 ± 19.6 × 10 -9 M( n = 5) in 1 × PBS bu ff er, using 1:1 Langmuir binding model.",step2c_acs_v1
365,Thrombin,protein,P00734,aptamer 2S,TATGGTTGGTGTGGTTGGATA,2.9400000000000002e-08 M,-7.532,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,SPR,,7.6,PBS buffer (pH 7.6) containing 138 mM NaCl and 2.7 mM KCl,,DNA,,32268723,10.1021/acs.analchem.0c00380,"The K d values of thrombin with aptamers 1S and 2S were calculated to be 1.08 μM and 29.4 nM, respectively",step2c_acs_v1
141,PDGF-C,protein,P01127,α-PC,CTACTGTGTGATGTCTGAGAGCAGCGTCTAAACGAACAAGCGAACCTATGCACAGAGGACAGTACATCAGACAC,33.0 nM,-7.481,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,,42138517,10.1167/iovs.67.5.36,SPR analysis demonstrated that the α -PC aptamer bound tightly to mouse PDGF-C with a high affinity ( KD = 33 nM,step2c_literal_v3
192,α-thrombin,protein,P00734,TBA-iT3,GGTTGGTGTGGTTGG,33.9 nM,-7.47,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,,100 mM KCl,,DNA,3'-inverted thymidine at position 3,30735210,10.1039/c9ob00053d,TBA-iT3 | 33.9,step2c_literal_v3
106,Human thrombin,protein,P00734,TBA29,TGACCCTAGTGACTGATTTACGAGGTC,36.9 nM,-7.433,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,backfill_text_verified,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,TBA29 | 1.34 10^5 | 4.94 10^-3 | 36.9,step2c_literal_v3
200,α-thrombin,protein,P00734,TBA-iT12,GGTTGGTGTGGTTGG,37.0 nM,-7.432,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,,100 mM KCl,,DNA,3'-inverted thymidine at position 12,30735210,10.1039/c9ob00053d,TBA-iT12 | 37.0,step2c_literal_v3
195,α-thrombin,protein,P00734,TBA-G8-iT8,GGTTGGTTTGGTTGG,37.1 nM,-7.431,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,7.4,"138 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, and 1.76 mM KH2PO4, pH 7.4, 0.05% Tween-20",,DNA,3'-inverted thymidine at position 8,30735210,10.1039/c9ob00053d,TBA-G8-iT8 | 37.1,step2c_literal_v3
112,rmCD3 d ε -Fc,protein,,CD3_Apt5,CCTTGCCTGCTTTCACGTGTGATCCCTGCCCGT,37.9 nM,-7.421,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,7.4,"PBS and 0.005% (v/v) Tween 20, pH 7.4",,2'F-RNA,2' Fluoropyrimidines,38745854,10.1016/j.omtn.2024.102198,aptamer 5 was the strongest binder (37.9 nM),step2c_literal_v3
197,α-thrombin,protein,P00734,TBA-iT9,GGTTGGTGTGGTTGG,41.0 nM,-7.387,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,7.4,"138 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, and 1.76 mM KH2PO4, pH 7.4, 0.05% Tween-20",,DNA,3'-inverted thymidine at position 9,30735210,10.1039/c9ob00053d,TBA-iT9 | 41.0,step2c_literal_v3
190,α-thrombin,protein,P00734,TBA,GGTTGGTGTGGTTGG,42.7 nM,-7.37,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,,100 mM KCl,,DNA,,30735210,10.1039/c9ob00053d,TBA | 42.7,step2c_literal_v3
199,α-thrombin,protein,P00734,TBA-iT12,GGTTGGTGTGGTTGG,46.8 nM,-7.33,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,7.4,"138 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, and 1.76 mM KH2PO4, pH 7.4, 0.05% Tween-20",,DNA,3'-inverted thymidine at position 12,30735210,10.1039/c9ob00053d,TBA-iT12 | 46.8,step2c_literal_v3
104,Human thrombin,protein,P00734,M08s,ACTGGAGATCACTGACTAAATGCTCCAG,47.2 nM,-7.326,intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,backfill_text_verified,KEEP_seq_in_figure,SPR,,7.4,"PBS [pH 7.4], 0.05 [v/v%] surfactant Tween 20",,DNA,,37621412,10.1016/j.omtn.2023.07.038,M08s | 7.04 10^5 | 3.33 10^-2 | 47.2,step2c_literal_v3
370,ODAM,protein,A1E959,OD64,,4.771e-08 M,-7.321,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_figure,,,SPR,,,,,DNA,,33455205,10.1021/acsbiomaterials.0c01203,"the obtained OD64 and OD35 (aptamer cognate pair) presented high a ffi nity and excellent speci fi city, along with dissociation constants ( K d ) of 47.71 nM (OD64)",step2c_acs_v1
371,ODAM,protein,A1E959,OD35,,5.1360000000000005e-08 M,-7.289,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_figure,,,SPR,,,,,DNA,,33455205,10.1021/acsbiomaterials.0c01203,"the obtained OD64 and OD35 (aptamer cognate pair) presented high a ffi nity and excellent speci fi city, along with dissociation constants ( K d ) of 47.71 nM (OD64) and 51.36 nM (OD35).",step2c_acs_v1
383,Aβ42 oligomer,protein,,Aβ-Apt,CGGTGGGGGACCAGTACAAAAGTGGGTAGGGCGGGTTGGAAAA,5.33e-08 M,-7.273,intrinsic,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,SPR,298.15,7.4,"1 × BB: 150 mM NaCl, 10 mM Tris -HCl, 5 mM KCl, 1 mM MgCl2, 1 mM CaCl2, pH 7.4",,DNA,,35019631,10.1021/acsabm.0c00996,suggesting that the binding a ffi nity of A β -Apt with A β 42 oligomer ( K d = 53.3 nM) was stronger than that of A β -Apt with A β 42 monomer.,step2c_acs_v1
191,α-thrombin,protein,P00734,TBA-iT3,GGTTGGTGTGGTTGG,57.3 nM,-7.242,non_intrinsic,Kd,Gold,v4,extraction_verified,verified_in_text_or_SI,original,,SPR,298.15,7.4,"138 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, and 1.76 mM KH2PO4, pH 7.4, 0.05% Tween-20",,DNA,3'-inverted thymidine at position 3,30735210,10.1039/c9ob00053d,TBA-iT3 | 57.3,step2c_literal_v3