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
724,Heparin-binding protein,protein,P21246,Apt-13,,1.04 nM,-8.983,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,38675537,10.3390/molecules29081717,"The KD values of the three aptamers were 3.42, 1.44, and 1.04 nM, respectively",elsevier_step2c
328,ATP,protein,P00846,Huizenga-Szostak ATP aptamer,,1.3e-09 M,-8.886,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_supp_oa,,,fluorescence,,,,,DNA,,25170558,10.1021/bc500286r,binding a ffi nity can be tuned over 4 orders of magnitude (1.3 nM -203 μ M),step2c_acs_v1
723,Heparin-binding protein,protein,P21246,Apt-02,,1.44 nM,-8.842,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,38675537,10.3390/molecules29081717,"The KD values of the three aptamers were 3.42, 1.44, and 1.04 nM, respectively",elsevier_step2c
63,CD8a,protein,P01732,A8,,5.59 nM,-8.253,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,binding buffer with 0.01% Tween 20,,DNA,,31209354,10.1038/s41551-019-0411-6,"the A1, A3 and A8 aptamers bound the protein with binding affinities ( K D values) of 20.1 ± 0.2,  14.7 ± 0.1  and  5.59 ± 0.11  nM, respectively",step2c_literal_v3
87,transferrin receptor 1,protein,P02786,JBA8.26,,6.87 nM,-8.163,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,,,,,DNA,,35875870,10.1021/jacs.2c05349,"Using BLI, JBA8.26 was found to bind immobilized TfR1 with a K D of 6.87 ± 0.04 nM",step2c_literal_v3
689,EN2,protein,P19622,EBA,,8.26 nM,-8.083,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35798816,10.1038/s41598-022-15556-1,EBA had K d =  8.26 nM (R 2 =  0.971),elsevier_step2c
697,β-conglutin,protein,,unmodified β-CBA II aptamer,,11.1 nM,-7.955,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,36354481,10.3390/bios12110972,"with a similar KD of 11.1 nM and 18.5 nM obtained for the unmodified and modified aptamer, respectively.",elsevier_step2c
62,CD8a,protein,P01732,A3,,14.7 nM,-7.833,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,binding buffer with 0.01% Tween 20,,DNA,,31209354,10.1038/s41551-019-0411-6,"the A1, A3 and A8 aptamers bound the protein with binding affinities ( K D values) of 20.1 ± 0.2,  14.7 ± 0.1  and  5.59 ± 0.11  nM, respectively",step2c_literal_v3
698,β-conglutin,protein,,biotinylated dUTPs aptamer,,18.5 nM,-7.733,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,36354481,10.3390/bios12110972,"with a similar KD of 11.1 nM and 18.5 nM obtained for the unmodified and modified aptamer, respectively.",elsevier_step2c
61,CD8a,protein,P01732,A1,,20.1 nM,-7.697,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,binding buffer with 0.01% Tween 20,,DNA,,31209354,10.1038/s41551-019-0411-6,"the A1, A3 and A8 aptamers bound the protein with binding affinities ( K D values) of 20.1 ± 0.2,  14.7 ± 0.1  and  5.59 ± 0.11  nM, respectively",step2c_literal_v3
677,saxitoxin,protein,O60939,45e,,21.2 nM,-7.674,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35324725,10.3390/toxins14030228,aptamer 45e with a K d value of 21.2 nM,elsevier_step2c
128,CD117,protein,P10721,Apta02,,21.8 nM,-7.662,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,,,DNA,,40487293,10.1002/adfm.202425394,"Apta02 and Apta04 exhibited K D 's of 21.8 nm and 1.10 µ m, respectively ( Figure 2 a,b).",step2c_literal_v3
86,transferrin receptor 1,protein,P02786,tJBA8.1,,25.11 nM,-7.6,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,,,,,DNA,biotinylated,35875870,10.1021/jacs.2c05349,tJBA8.1 bound the TfR1 protein with a K D value of 25.11 ± 0.19 nM,step2c_literal_v3
716,Enrofloxacin,protein,P05177,ENR-Apt 6,,35.08 nM,-7.455,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,38540931,10.3390/foods13060941,"Figure 4A shows the non-linear fitting curve of ENR-Apt 6, with a Kd value of 35.08 nM.",elsevier_step2c
97,N-acetylneuraminic acid,protein,Q8NFW8,Neu5Ac aptamer,,91.0 nM,-7.041,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,ITC,310.15,7.4,"1× aptamer binding buffer (50 mM Tris-HCl, 5 mM KCl, 100 mM NaCl and 1 mM MgCl2, pH 7.4)",1.0,DNA,,37217750,10.1038/s41587-023-01801-z,"To validate ARPLA, we first determined the binding affinity ( K d ) of the Neu5Ac aptamer by isothermal titration calorimetry (ITC) as 91 nM (Extended Data Fig. 2a,b)",step2c_literal_v3
687,mouse IL-2,protein,,M20,,91.0 nM,-7.041,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35756119,10.1016/j.heliyon.2022.e09721,"The results indicated that the af fi nity of the M20 aptamer was greater than the M15, and its predicted Kd was 91 nM",elsevier_step2c
678,saxitoxin,protein,O60939,75a,,136.0 nM,-6.866,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35324725,10.3390/toxins14030228,aptamer 75a with a K d value of 136 nM,elsevier_step2c
419,cortisol,protein,P08185,CSS.3,,2.4000000000000003e-07 M,-6.62,intrinsic,Kd,Gold,v4,multi_agent_verified,pending_supp_oa,,,,,,,,,,38270529,10.1021/acssensors.3c02004,Our own internal work confirmed that CSS.3 had the best binding affinity in binding buffer with a K D of 240 nM,step2c_acs_v1
673,kanamycin,protein,,Apt 1/Apt 2 (split aptamers),,247.0 nM,-6.607,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35316405,10.1007/s00604-022-05235-3,"With the (GlcN)5 added in the binding buffer, the Kd was measured to be 247 nM",elsevier_step2c
672,kanamycin,protein,,Apt 1/Apt 2 (split aptamers),,304.0 nM,-6.517,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35316405,10.1007/s00604-022-05235-3,"The split aptamers exhibited high affinity towards the kanamycin, with an Kd of 304 nM.",elsevier_step2c
688,mouse IL-2,protein,,M15,,600.0 nM,-6.222,intrinsic,Kd,Gold,elsevier,extraction_verified,pending_supp_oa,,,,,,text,,,,35756119,10.1016/j.heliyon.2022.e09721,"The calculation of the dissociation constant predicted 91 and 600 nM Kd for M20 and M15, respectively",elsevier_step2c
129,CD117,protein,P10721,Apta04,,1100.0 nM,-5.959,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,,,DNA,,40487293,10.1002/adfm.202425394,"Apta02 and Apta04 exhibited K D 's of 21.8 nm and 1.10 µ m, respectively ( Figure 2 a,b).",step2c_literal_v3
131,CD123,protein,O75794,Apta25,,1.16 µM,-5.936,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,,,DNA,,40487293,10.1002/adfm.202425394,"BLI binding assays of both aptamers demonstrated binding to human recombinant CD123 with K D s of 1.16 µ m for ZW25 and 15.6 µ m for CY30 (Figure S2, Supporting Information).",step2c_literal_v3
121,CTNNA1,protein,P35221,EA2,,2.07 µM,-5.684,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,MST,,,,,DNA,biotinylated,40265971,10.1002/advs.202411930,The K d values (2.07 ± 0.60 µ M) obtained from MST assay (Figure 2l) further corroborated the specific binding between CTNNA1 and EA2.,step2c_literal_v3
130,CD123,protein,O75794,Apta30,,15.6 µM,-4.807,intrinsic,Kd,Gold,v4,extraction_verified,pending_supp_oa,,,BLI,298.15,,,,DNA,,40487293,10.1002/adfm.202425394,"BLI binding assays of both aptamers demonstrated binding to human recombinant CD123 with K D s of 1.16 µ m for ZW25 and 15.6 µ m for CY30 (Figure S2, Supporting Information).",step2c_literal_v3