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
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
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
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
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
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
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
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
50,PDGF-BB,protein,P01127,PDGF-specific aptamer,,5e-10 M,-9.301,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,microcantilever,310.15,7.4,"PBSM buffer (10.1 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, and 1 mM MgCl2, pH 7.4)",1.0,DNA,3'-3'-linked thymidine nucleotide ([3'T]); thiolated 5'-end,24723743,10.1016/j.snb.2012.02.045,"K d , as shown in Fig. 10, decreased from approximately 12 × 10 -10 M to 5 × 10 -10 M as the temperature changed from 19 to 37 ◦ C.",step2c_literal_v3
4,sLe X -BSA,glycan/conjugate,Q9NSU2,Clone 2,,8e-10 M,-9.097,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,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,Clone 2 | 9.8 3 10 5 | 7.3 3 10 2 5 | 1.2 3 10 9 | 8.0 3 10 2 10,step2c_literal_v3
150,P-selectin,protein,Q14242,PF422sl,,1000.0 pM,-9.0,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,PF422sl | 1 X 103,step2c_literal_v3
49,PDGF-BB,protein,P01127,PDGF-specific aptamer,,1.2e-09 M,-8.921,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,microcantilever,292.15,7.4,"PBSM buffer (10.1 mM Na2HPO4, 1.8 mM KH2PO4, 137 mM NaCl, 2.7 mM KCl, and 1 mM MgCl2, pH 7.4)",1.0,DNA,3'-3'-linked thymidine nucleotide ([3'T]); thiolated 5'-end,24723743,10.1016/j.snb.2012.02.045,"K d , as shown in Fig. 10, decreased from approximately 12 × 10 -10 M to 5 × 10 -10 M as the temperature changed from 19 to 37 ◦ C.",step2c_literal_v3
215,CD8,protein,P01732,CD8 aptamer,,1.9 nM,-8.721,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,flow_cytometry,,,,,DNA,3'-toehold extension,32786336,10.1021/acs.accounts.0c00335,"The aptamer with the highest apparent affinity (1.9 nM) and association rate, measured by flow cytometry and biolayer interferometry, respectively, was chosen for further use in cell isolation.",step2c_literal_v3
31,VWF A1-domain,protein,P04275,ARC1779,,2.0 nM,-8.699,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,filter_binding,298.15,,Dulbecco's PBS containing 0.1 mg mL-1 BSA,,DNA/RNA,2'-O-methyl; phosphorothioate; inverted deoxythymidine; 20-kDa PEG conjugation,19422452,10.1111/j.1538-7836.2009.03459.x,This resulted in a final aptamer (ARC1779) that is a 40-nucleotide modified DNA/RNA oligonucleotide with a K D of 2 nM for the A1-domain.,step2c_literal_v3
64,von Willebrand factor,protein,P04275,42-nt DNA aptamer,,2.0 nM,-8.699,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,FLAG_cited_data,ELISA,,,PBS with 1% BSA,,DNA,biotinylated,31493779,10.1055/s-0039-1696713,a biotinylated DNA aptamer was able to bind an antibody-captured VWF in a concentration-dependent manner with a dissociation constant ( KD ) of 2.0 nM  0.3.,step2c_literal_v3
157,von Willebrand factor A1 domain,protein,P04275,ARC1779,,2.0 nM,-8.699,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,,,,,,,DNA,20-kDa polyethylene glycol conjugation; nuclease-resistant,21108551,10.1586/erc.10.154,ARC1779 binds with high affinity (Kd ~ 2 nM) to the vWF A1 domain,step2c_literal_v3
5,sLe X -BSA,glycan/conjugate,Q9NSU2,Clone 15,,2.3e-09 M,-8.638,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,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,Clone 15 | 3.5 3 10 5 | 8.1 3 10 2 4 | 4.3 3 10 8 | 2.3 3 10 2 9,step2c_literal_v3
702,melatonin,protein,P48039,MLT-A-2,,2.4 nM,-8.62,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_figure,,,,,,text,,,,36925277,10.1016/j.aca.2023.340971,K d = 2.4 ± 2.8 nM for MLT-A-2,elsevier_step2c
705,melatonin,protein,P48039,MLT-A-2F,,2.4 nM,-8.62,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_figure,,,,,,abstract,,,,36925277,10.1016/j.aca.2023.340971,MLT-A-2F K d = 2.4 ± 2.8 nM,elsevier_step2c
545,Human Cardiac Troponin I,protein,P19429,TnIApt 23,,2.69 nM,-8.57,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_figure,,,,,,abstract,,,,26003883,10.1016/j.jbiotec.2015.05.002,Finally TnIApt 23 showed beast affinity in nanomolar range (2.69 nM) toward the target protein.,elsevier_step2c
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
6,sLe X -BSA,glycan/conjugate,Q9NSU2,Clone 18,,3.9e-09 M,-8.409,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,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,Clone 18 | 5.1 3 10 5 | 2.0 3 10 2 3 | 2.5 3 10 8 | 3.9 3 10 2 9,step2c_literal_v3
7,sLe X -BSA,glycan/conjugate,Q9NSU2,Clone 4,,7.4e-09 M,-8.131,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,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,Clone 4 | 4.1 3 10 5 | 3.1 3 10 2 3 | 1.3 3 10 8 | 7.4 3 10 2 9,step2c_literal_v3
569,MPT64,protein,,aptamer sequence (17),,8.92 nM,-8.05,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_figure,,,,,,text,,,,28454652,10.1016/j.tube.2017.03.004,KD (dissociation equilibrium constant) was 8.92 nM,elsevier_step2c
8,sLe X -BSA,glycan/conjugate,Q9NSU2,Clone 9,,1e-08 M,-8.0,intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,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,Clone 9 | 3.5 3 10 5 | 3.1 3 10 2 3 | 9.5 3 10 7 | 1.0 3 10 2 8,step2c_literal_v3
704,N-acetyl-5-hydroxytryptamine,protein,P46597,MLT-A-4F,,0.016 μM,-7.796,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_figure,,,,,,text,,,,36925277,10.1016/j.aca.2023.340971,"for NAT very low K d value was observed i.e., 0.016 μM",elsevier_step2c
336,VEGF-165,protein,P15692,bivalent construct for VEGF-165 (no linker),,1.7e-08 M,-7.77,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,pending_manual_figure,,,,,,,,,,27043498,10.3390/molecules21040421,this bivalent construct had about 28-fold higher binding affinity ( K D = 17 nM),step2c_acs_v1
377,dT35,protein,,DCC-SSB,,2.9e-08 M,-7.538,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_figure,,,,,,,,,,34085169,10.1007/s12010-021-03585-x,The second stage was fitted to a hyperbola to give a K d value of 29 nM.,step2c_acs_v1
158,Mycobacterium tuberculosis H37Rv,protein,,NK2,,31.0 nM,-7.509,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,KEEP_seq_in_figure,flow_cytometry,,,PBS,,DNA,FITC,21643749,10.1007/s11033-011-0963-3,| NK2    | 31 ± 4 |,step2c_literal_v3
346,Ciprofloxacin,protein,Q86VL8,R10K6,,3.1e-08 M,-7.509,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_figure,,,,,,,,,,30609709,10.3390/bios9010007,a dissociation constant (KD) for the RNA-ligand complex of 31 nM was determined.,step2c_acs_v1
160,Mycobacterium tuberculosis H37Rv,protein,,NK7,,35.0 nM,-7.456,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,KEEP_seq_in_figure,flow_cytometry,,,PBS,,DNA,FITC,21643749,10.1007/s11033-011-0963-3,| NK7    | 35 ± 9 |,step2c_literal_v3
347,Ciprofloxacin,protein,Q86VL8,R10K6_V11,,3.6000000000000005e-08 M,-7.444,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_figure,,,,,,,,,,30609709,10.3390/bios9010007,The determined dissociation constant of 36 nM for V11 is similar to the original full-length aptamer R10K6 (31 nM).,step2c_acs_v1
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
159,Mycobacterium tuberculosis H37Rv,protein,,NK1,,48.0 nM,-7.319,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,KEEP_seq_in_figure,flow_cytometry,,,PBS,,DNA,FITC,21643749,10.1007/s11033-011-0963-3,| NK1     | 48 ± 13 |,step2c_literal_v3
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
163,Mycobacterium tuberculosis H37Rv,protein,,NK20,,55.0 nM,-7.26,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,KEEP_seq_in_figure,flow_cytometry,,,PBS,,DNA,FITC,21643749,10.1007/s11033-011-0963-3,| NK20    | 55 ± 16 |,step2c_literal_v3
162,Mycobacterium tuberculosis H37Rv,protein,,NK10,,95.0 nM,-7.022,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,KEEP_seq_in_figure,flow_cytometry,,,PBS,,DNA,FITC,21643749,10.1007/s11033-011-0963-3,| NK10    | 95 ± 28 |,step2c_literal_v3
161,Mycobacterium tuberculosis H37Rv,protein,,NK8,,107.0 nM,-6.971,non_intrinsic,Kd,Gold,v4,extraction_verified,pending_manual_figure,,KEEP_seq_in_figure,flow_cytometry,,,PBS,,DNA,FITC,21643749,10.1007/s11033-011-0963-3,| NK8      | 107 ± 44 |,step2c_literal_v3
379,dT20,protein,,DCC-SSB,,2.4000000000000003e-07 M,-6.62,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_figure,,,,293.15,,,,,,34085169,10.1007/s12010-021-03585-x,"Titrations of dT 27 and dT20 at low concentrations of DCCSSB gave smaller fluorescence changes, and the data were fit to give single K d values of 43 and 240 nM, respectively",step2c_acs_v1
703,5-Methoxytryptamine,protein,P48039,MLT-C-1F,,0.274 μM,-6.562,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_figure,,,,,,text,,,,36925277,10.1016/j.aca.2023.340971,"For L-TRP and 5-MT very low K d were observed i.e., 0.324 μM and 0.274 μM respectively",elsevier_step2c
380,dT20,protein,,DCC-SSB,,3.96e-07 M,-6.402,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_manual_figure,,,,293.15,,,,,,34085169,10.1007/s12010-021-03585-x,"With dT20, the intercept suggests a dissociation rate constant of 49 s -1 , producing a value of 396 nM for the equilibrium dissociation constant",step2c_acs_v1
563,Brevetoxin-2,protein,,Bap5,,4.83 uM,-5.316,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_manual_figure,,,,,,text,,,,28058132,10.1155/2016/9241860,The Kd value for the binding between the Bap5 aptamer and BTX-2 was 4.83 uM,elsevier_step2c
151,P-selectin,protein,Q14242,NX244,,9000000.0 pM,-5.046,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,NX244 | 9 X 106,step2c_literal_v3