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
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
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
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
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
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
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
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