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
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
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
434,Ara h1,protein,P35354,CB-APT1,GTGCTCGGACTCCACTTGCGCTTCATTAACCGGGTTGCTCATTTATTCA,3.63e-08 M,-7.44,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,MST,298.15,7.2,1 × binding buffer,,DNA,,40083221,10.1021/acs.analchem.5c00270,"Among them, CBAPT1 exhibited the strongest binding to Ara h1 with a K d value of 36.3 nM in aqueous solutions.",step2c_acs_v1
435,Ara h1,protein,P35354,CB-APT1,GTGCTCGGACTCCACTTGCGCTTCATTAACCGGGTTGCTCATTTATTCA,4.5000000000000006e-08 M,-7.347,avidity_multivalent,Kd,Gold,v4,multi_agent_verified,verified_in_text_or_SI,original,,MST,298.15,7.2,1 × binding buffer with 80% w/w total peanut proteins,,DNA,,40083221,10.1021/acs.analchem.5c00270,"Notably, a similar binding affinity was observed even in a complex matrix that contained 80% w/w total peanut proteins ( K d = 45.0 nM, Figures 3 and S5).",step2c_acs_v1