Binding affinities (Kd) — source-verified (view)
Data license: CC BY 4.0 · Data source: apt-scout automated curation pipeline (E. Dohi, NCNP) — values harvested from public databases; raw source stored per target
- target_name_canonical
- Target as named in the source paper.
- target_type
- protein / cell-line+EV / glycan-conjugate. Filter to 'protein' for molecular targets.
- target_uniprot
- UniProt accession when a human protein (sparse for now; links to apt-scout target).
- aptamer_name
- Aptamer identifier as reported.
- kd_reported
- Kd value AS REPORTED in the paper (value + unit). Units are MIXED — do NOT compare this column directly.
- kd_log10_molar
- log10(Kd in molar). THE column to sort / compare / learn on (lower = tighter).
- measurement_class
- intrinsic = equilibrium vs purified target; non_intrinsic = apparent/cellular or avidity (NOT comparable to intrinsic).
- binding_constant_type
- Kd / apparent-Kd etc. as reported.
- assay_method
- SPR / filter binding / flow cytometry / ITC / BLI …
- assay_temperature_k
- Assay temperature (K) — a reason the same pair can have several rows.
- source_pmid
- PubMed ID of the source paper (links out).
- verbatim_quote
- The exact sentence the value was taken from.
- verification_level
- QC status (honest, growing): human_verified / human_corrected = a logged human verdict from the stratified-random sample; multi_agent_verified = passed independent multi-agent (L2) check; extraction_verified = extraction-pipeline verified; automated. Human verification is in progress: as of this release 0 records carry a logged human verdict — the published set is multi-agent-/extraction-verified, and human spot-checking is being added post-publication (version-tracked). No record is labelled human_verified without a logged human review.
- sequence_status
- Aptamer-sequence provenance: verified_in_text_or_SI = sequence verbatim-verified against the source text/SI (shown); pending_manual_supp / pending_supp_oa / pending_manual_figure = sequence reported only in a (often paywalled) SI or a figure, being curated post-submission; no_single_sequence_pool = a pool/library/primer, no single sequence exists.
- pi_provenance_flag
- PI manual-review flag: KEEP_seq_in_figure = valid record, sequence is in a 3D-structure figure; FLAG_cited_data = Kd may be a value cited from elsewhere, re-verify. (EXCLUDE rows are hidden from this view.)
- seq_source
- original (already in source DB) / backfill_text_verified (recovered from paper or SI text).
113 rows where sequence_status = "verified_in_text_or_SI" and verification_level = "multi_agent_verified" sorted by kd_log10_molar
This data as json, CSV (advanced)
Suggested facets: source_origin, seq_source, assay_temperature_k, assay_ph, assay_buffer, aptamer_chemistry, aptamer_modifications
assay_method 13
- fluorescence 13
- SPR 8
- affinity_real_time_qPCR 8
- flow_cytometry 8
- MST 6
- BLI 3
- PISA 3
- ITC 2
- QCM 2
- ALISA 1
- ELAA 1
- NECEEM 1
- saturation_binding 1
measurement_class 4
verification_level 1
- multi_agent_verified · 113 ✖
tier 1
- Gold 113
target_type 1
- protein 113
sequence_status 1
- verified_in_text_or_SI · 113 ✖
binding_constant_type 1
- Kd 113
| 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 | |||
| 331 | MutS | protein | O15457 | 2-06 | ACTTCTGCCCGCCTCCTTCCTGGTAAAGTCATTAATAGGTGTGGGGTGCCGGGCATTTCGGAGACGAGATAGGCGGACACT | 1.23e-10 M | -9.91 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | 25668425 | 10.1021/acs.analchem.5b00171 | The best fi t was obtained at K d = 123 pM and [T]0 = 213 pM | step2c_acs_v1 | ||||||||
| 363 | HBcAg | protein | A-9 | AGCAGCACAGAGGTCAGATGAGGCCTGGTGATCGTGCCCAGGCCATATGAGCAAGGAACCCCTATGCGTGCTACCGTGAA | 2.0000000000000003e-10 M | -9.699 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | affinity_real_time_qPCR | DNA | 32250595 | 10.1021/acs.analchem.9b05740 | This aptamer showed strong binding to HBcAg ( K d : 0.2 nM) | step2c_acs_v1 | |||||||
| 318 | VEGF165 | protein | P15692 | 3R02 | TGTGGGGGTGGACTGGGTGGGTACC | 3e-10 M | -9.523 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | 23237717 | 10.1021/ac303023d | The K d value for 3R02 was 300 pM | step2c_acs_v1 | ||||||||
| 358 | HBeAg | protein | EAg3-Py | TTTTTTTTGGGCGAAGACCGGGACGGGAGGAAAGAGATGTTTGGTTTT | 4.0000000000000007e-10 M | -9.398 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | affinity_real_time_qPCR | 7.4 | 1 × BB (50 mM Tris-HCl (pH 7.4), 5 mM KCl, 50 mM NaCl, 7 mM MgCl2, and 0.05% Tween 20) | DNA | pyrrolo-dC | 32250595 | 10.1021/acs.analchem.9b05740 | The K d value is 0.4 nM for the HBeAg complex with the pyrrolo-dC modi fi ed aptamer EAg3 | step2c_acs_v1 | ||||
| 415 | BDNF | protein | P23560 | NV_B12 | GGATTTGAGCTTATGTGGCATAGGTTGCCTGGGTGGGTGGGGTCGGGGAA | 5e-10 M | -9.301 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | ALISA | 1 × selection buffer | DNA | biotin | 38149631 | 10.1021/acschemneuro.3c00661 | The equilibrium dissociation constant ( K d) for the NV_B12/BDNF interaction was obtained by fitting the equation, Y = B max × X /( K d + X )... The K d value determined to be 0.5 nM (95% CI: 0.4 -0.6 nM) | step2c_acs_v1 | ||||
| 343 | PlanarAu | protein | 1N | TATGCATGTGTAGTAAGACCTAGTCCACAATCAACG | 5.600000000000001e-10 M | -9.252 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | QCM | AIB | DNA | 30189130 | 10.1021/acscombsci.8b00048 | aptamer 1N showing the highest affinity (0.56 nM) | step2c_acs_v1 | ||||||
| 332 | MutS | protein | O15457 | 2-06 | ACTTCTGCCCGCCTCCTTCCTGGTAAAGTCATTAATAGGTGTGGGGTGCCGGGCATTTCGGAGACGAGATAGGCGGACACT | 6.5e-10 M | -9.187 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | 25668425 | 10.1021/acs.analchem.5b00171 | The experimental points from the second step resulted in the best fi t with the theoretical dependence of R versus [L] 0 at K d = 650 pM | step2c_acs_v1 | ||||||||
| 398 | neomycin | protein | Q96LI5 | Aptamer A | GGACUGGGCGAGAAGUUUAGUCC | 1e-09 M | -9.0 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | 36453647 | 10.1021/acschembio.2c00653 | The binding affinity of neomycin to Aptamer A shows a strong K d of 1 nM with an enthalpy and entropy value of -100 kJ/mol & -163.1 J/mol. K | step2c_acs_v1 | ||||||||
| 432 | Sc3+ | protein | Q96PL5 | Sc-1 | CTCTCGACGACGGACCATTCCCGTGGAATGACTACGTATATGTCGTC | 1e-09 M | -9.0 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | fluorescence | SELEX buffer | DNA | 39743479 | 10.1021/jacs.4c13768 | true K d for the binding of Sc-1 to Sc 3+ to be 1.0 nM | step2c_acs_v1 | |||||
| 372 | beta-conglutin | protein | 11-mer | GGTGGGGGTGG | 1.05e-09 M | -8.979 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | MST | 298.15 | binding buffer with 0.05% v/v Tween-20 | DNA | 33498970 | 10.3390/ijms22031150 | KD values determined (Figure 6b) are very similar (11-mer: 1.05 nM | step2c_acs_v1 | |||||
| 340 | AP65 | protein | Q13882 | AP65_A1 | AGCTCCAGAAGATAAATTACAGGTGAGGGCGGGCGGGTGGTTGTAATATGATCGAATGGTATATGTGTGTTTGCAACTAGGATACTATGACCCCG | 1.057e-09 M | -8.976 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | ELAA | 298.15 | 6.4 | binding buffer (10 mM phosphate, 138 mM NaCl, 2.7 mM KCl, 1.5 mM MgCl2 at pH 6.4) | DNA | 5'-biotinylated | 29972299 | 10.1021/acsinfecdis.8b00065 | A K D value of 1.057 nM was obtained using the sigmoidal dose-response curve model | step2c_acs_v1 | ||
| 356 | HBeAg | protein | A-9S | ACTTTTTTGGTCAGATGAGGCCTGGTGATCGTGCCCAGGCCATATGAGCAAGGAACCCCTATGCGTGCT | 1.2e-09 M | -8.921 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | affinity_real_time_qPCR | 7.4 | 1 × BB (50 mM Tris-HCl (pH 7.4), 5 mM KCl, 50 mM NaCl, 7 mM MgCl2, and 0.05% Tween 20) | DNA | /5AmMC6/ | 32250595 | 10.1021/acs.analchem.9b05740 | The measured dissociation constant ( K d) is improved by 19 times from a K d value of 22.9 nM with the 80-nt sequence to a K d of 1.2 nM with the new 61-nt aptamer. | step2c_acs_v1 | ||||
| 433 | PvTRAg | protein | Apt_16 | TTAATAACATGAGTTATTGAATTATTGTTTATTTTTTTTTTTTTG | 1.2e-09 M | -8.921 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | DNA | 40042916 | 10.1021/acsinfecdis.4c01047 | The K D of Apt_14 and Apt_16 was found to be comparable, 1.9 and 1.2 nM, respectively | 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 | |||||
| 394 | IgE | protein | P0DOX4 | S2 | GACTACCCGGGTATCTAATCCGACCATTTTTCGTCTCCTTTGTACGAGCAGTGTGCTCGACCTGCCGCCCGTAGG | 1.5500000000000002e-09 M | -8.81 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | NECEEM | 9.0 | 10 mM Tris-HCl buffer (pH 9.0) | DNA | FITC | 36144553 | 10.3390/molecules27185818 | Based on the results of these experiments, the K D values of S1 and S2 were estimated to be 0.83 and 1.55 nM, respectively | step2c_acs_v1 | |||
| 359 | HBeAg | protein | EAg3 | TTTTTTTTGGGCGAAGACCGGGACGGGAGGAAAGAGATGTTTGGTTTT | 1.7000000000000001e-09 M | -8.77 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | affinity_real_time_qPCR | 7.4 | 1 × BB (50 mM Tris-HCl (pH 7.4), 5 mM KCl, 50 mM NaCl, 7 mM MgCl2, and 0.05% Tween 20) | DNA | 32250595 | 10.1021/acs.analchem.9b05740 | The K d value is 0.4 nM for the HBeAg complex with the pyrrolo-dC modi fi ed aptamer EAg3, as compared to the K d value of 1.7 nM with the unmodi fi ed EAg3 aptamer. | step2c_acs_v1 | |||||
| 374 | beta-conglutin | protein | TT-11-mer | TTGGTGGGGGTGG | 1.88e-09 M | -8.726 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | MST | 298.15 | binding buffer with 0.05% v/v Tween-20 | DNA | 33498970 | 10.3390/ijms22031150 | KD values determined (Figure 6b) are very similar (... TT-11 mer: 1.88 nM | step2c_acs_v1 | |||||
| 376 | beta-conglutin | protein | 11-mer-TT | GGTGGGGGTGGTT | 2.59e-09 M | -8.587 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | MST | 298.15 | binding buffer with 0.05% v/v Tween-20 | DNA | 33498970 | 10.3390/ijms22031150 | KD values determined (Figure 6b) are very similar (... and 11-mer-TT: 2.59 nM) | step2c_acs_v1 | |||||
| 375 | beta-conglutin | protein | TT-11-mer-TT | TTGGTGGGGGTGGTT | 2.71e-09 M | -8.567 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | MST | 298.15 | binding buffer with 0.05% v/v Tween-20 | DNA | 33498970 | 10.3390/ijms22031150 | KD values determined (Figure 6b) are very similar (... TT-11-mer-TT: 2.71 nM | step2c_acs_v1 | |||||
| 367 | SARS-CoV-2 RBD | protein | CoV2-RBD-1 | CAGCACCGACCTTGTGCTTTGGGAGTGCTGGTCCAAGGGCGTTAATGGACA | 3.1000000000000005e-09 M | -8.509 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | backfill_text_verified | flow_cytometry | PBS with 0.55 mM MgCl2 | DNA | 32551560 | 10.1021/acs.analchem.0c01394 | the dissociation constant values ( K d) of the CoV2-RBD-1 aptamer ... were 3.1 nM | step2c_acs_v1 | ||||||
| 410 | melamine | protein | Apt M | TTCCTTTTCTCTCC | 4.4000000000000005e-09 M | -8.357 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | backfill_text_verified | DNA | abasic site | 37343019 | 10.1021/acs.analchem.2c05777 | dissociation constant K d = 4.4 nM | step2c_acs_v1 | |||||||
| 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 | |||
| 327 | Myoglobin | protein | P02144 | Myo40-7-27 | CCCTCCTTTCCTTCGACTAGATCTGCTGCGTTGTTCCGA | 4.93e-09 M | -8.307 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | DNA | 24914856 | 10.1021/ac501088q | The aptamer with the highest a ffi nity ( K d = 4.93 nM) was then used for the fabrication of a label-free supersandwich electrochemical biosensor for Myo detection | step2c_acs_v1 | |||||||
| 455 | biliverdin | protein | P53004 | Bvd4 | GACGACGGGTGTGGAACAGTGCGAATACTTTCGAGTCGTC | 6.000000000000001e-09 M | -8.222 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | 40669049 | 10.1021/acschembio.5c00438 | For the biliverdin selection, the tightest affinity aptamer has a dissociation costant ( K d ) value of 6 nM determined using isothermal titration calorimetry (ITC) | step2c_acs_v1 | ||||||||
| 313 | Salmonella enteritidis | protein | P29460 | SENT-9 | CTCCTCTGACTGTAACCACGCACAAAGGCTCGCGCATGGTGTGTACGTTCTTACAGAGGT | 7.000000000000001e-09 M | -8.155 | apparent_cellular | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | 22971146 | 10.1021/ac302217u | It was observed that the aptamer pool collected at the seventh round of selection had the highest binding a ffi nity to the bacteria ( K D = 7 nM). | step2c_acs_v1 | ||||||||
| 445 | Cu2+ | protein | Q6UVY6 | Co-1 | GACGACGGAACGGAGGTTCTTAGGTCGGTAGACCGAGTCGTC | 8e-09 M | -8.097 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | 40656531 | 10.1039/d5sc02436f | The corresponding true K d values were ... 8 nM for Cu 2+ | step2c_acs_v1 | ||||||||
| 309 | Streptococcus pyogenes M-type mixture | protein | 20A24P | AAGCAGCACAGAGGTCAGATGGGGGGAAGACACAGAGAAAGGCCGGGGTGAAGTGTAGAGGCCTATGCGTGCTACCGTGAA | 9.000000000000001e-09 M | -8.046 | apparent_cellular | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | flow_cytometry | 7.4 | binding buffer (1-BB; 50 mM Tris-HCl(pH7.4), 5 mM KCl, 100 mM NaCl, 1 mM MgCl2) | DNA | 5'-FAM | 21504182 | 10.1021/ac200575e | Two aptamers, 20A24P and 15A3P (with estimated binding dissociation constants of 9 and 10 nM, respectively) | step2c_acs_v1 | ||||
| 362 | HBeAg | protein | EAg2 | TTTTTTTTGGGCGAAGACCGGGACGGGAGGAAAGTGTAGATTGGAAAA | 9.2e-09 M | -8.036 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | affinity_real_time_qPCR | 7.4 | 1 × BB (50 mM Tris-HCl (pH 7.4), 5 mM KCl, 50 mM NaCl, 7 mM MgCl2, and 0.05% Tween 20) | DNA | 32250595 | 10.1021/acs.analchem.9b05740 | A comparison of the binding of HBeAg with the four aptamers (Figure S3) shows K d values of 44.2 nM for EAg0, 9.5 nM for EAg1, 9.2 nM for EAg2 | step2c_acs_v1 | |||||
| 361 | HBeAg | protein | EAg1 | TTTTTTTTGGGCGAAGACCGGGACGGGAGGAAAGTGTAGATTGGTTTT | 9.5e-09 M | -8.022 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | affinity_real_time_qPCR | 7.4 | 1 × BB (50 mM Tris-HCl (pH 7.4), 5 mM KCl, 50 mM NaCl, 7 mM MgCl2, and 0.05% Tween 20) | DNA | 32250595 | 10.1021/acs.analchem.9b05740 | A comparison of the binding of HBeAg with the four aptamers (Figure S3) shows K d values of 44.2 nM for EAg0, 9.5 nM for EAg1 | step2c_acs_v1 | |||||
| 310 | Streptococcus pyogenes M-type mixture | protein | 15A3P | ATTCACGGTAGCACGCATAGGGACAGCAAGCCCAAGCTGGGTGTGCAAGGTGAGGAGTGGG | 1e-08 M | -8.0 | apparent_cellular | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | flow_cytometry | 7.4 | binding buffer (1-BB; 50 mM Tris-HCl(pH7.4), 5 mM KCl, 100 mM NaCl, 1 mM MgCl2) | DNA | 5'-FAM | 21504182 | 10.1021/ac200575e | Two aptamers, 20A24P and 15A3P (with estimated binding dissociation constants of 9 and 10 nM, respectively) | step2c_acs_v1 | ||||
| 431 | Sc3+ | protein | Q96PL5 | Sc-1 | CTCTCGACGACGGACCATTCCCGTGGAATGACTACGTATATGTCGTC | 1.0300000000000001e-08 M | -7.987 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | fluorescence | SELEX buffer | DNA | 39743479 | 10.1021/jacs.4c13768 | an apparent K d value of 10.3 nM was obtained | step2c_acs_v1 | |||||
| 427 | U87MG GBM with IDH1 htz mutation | protein | Gli-55 | GTCCGGTTCAACCTCTAGCATTCCTGGCGTTATTAACGGAGCAGTCCTGTGGAGTGGGTGA | 1.22e-08 M | -7.914 | apparent_cellular | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | flow_cytometry | 298.15 | DPBS | DNA | Cy5 | 39682297 | 10.3390/cancers16234111 | The apparent dissociation constant measured for U87MG GBM with the IDH1 htz mutation ( Kd ) of Gli-55 is 12.2 nM | step2c_acs_v1 | ||||
| 344 | PlanarAu | protein | 1N truncated | TATGCATGTGTATATCAACACTCCGGGTCTAATCGTTCA | 1.304e-08 M | -7.885 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | QCM | AIB | DNA | 30189130 | 10.1021/acscombsci.8b00048 | 1N truncated (Kd = 13.04 nM) | step2c_acs_v1 | ||||||
| 368 | SARS-CoV-2 RBD | protein | CoV2-RBD-4 | ATCCAGAGTGACGCAGCATTTCATCGGGTCCAAAAGGGGCTGCTCGGGATTGCGGATATGGACACGT | 1.3600000000000001e-08 M | -7.866 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | backfill_text_verified | flow_cytometry | PBS with 0.55 mM MgCl2 | DNA | 32551560 | 10.1021/acs.analchem.0c01394 | the dissociation constant values ( K d) of the ... CoV2-RBD-4 aptamer ... were ... 13.6 nM | step2c_acs_v1 | ||||||
| 428 | U87MG GBM with IDH1 htz mutation | protein | Gli-35 | GCGTTATTAACGGAGCAGTCCTGTGGAGTGGGTGA | 1.3600000000000001e-08 M | -7.866 | apparent_cellular | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | flow_cytometry | 298.15 | DPBS | DNA | Cy5 | 39682297 | 10.3390/cancers16234111 | while for Gli-35, it is 13.6 nM. | step2c_acs_v1 | ||||
| 476 | Escherichia coli O157:H7 | protein | E. coli O157:H7-specific aptamer | CCGGACGCTTATGCCTTGCCATCTACAGAGCAGGTGTGACGG | 1.4400000000000002e-08 M | -7.842 | apparent_cellular | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | fluorescence | 298.15 | 15% (v/v) PEG200 | DNA | FAM | 41850902 | 10.1021/acs.analchem.5c07364 | the aptamer exhibited enhanced binding affinity in the crowded microenvironment, with a 25% reduction in Kd (from 19.2 to 14.4 nM). | step2c_acs_v1 | ||||
| 411 | thrombin | protein | P00734 | TBA15-AnBtz | GGTTGGTGTGGTTGGTATATT | 1.5000000000000002e-08 M | -7.824 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | 37857354 | 10.1021/acs.bioconjchem.3c00373 | apparent dissociation constant ( K d ) of 15 nM | step2c_acs_v1 | ||||||||
| 330 | Progesterone | protein | P06401 | P4G13 | GCATCACACACCGATACTCACCCGCCTGATTAACATTAGCCCACCGCCCACCCCCGCTGC | 1.7e-08 M | -7.77 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | 25486123 | 10.1021/ac503639s | The dissociation constant of the best aptamer, designated as P4G13, was estimated to be 17 nM by electrochemical impedance spectroscopy (EIS) as well as fl uorometric assay. | step2c_acs_v1 | ||||||||
| 421 | hnRNP A1 | protein | P09651 | AS1411 | GGTGGTGGTGGTTGTGGTGGTGGTGG | 1.75e-08 M | -7.757 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | BLI | 7.4 | BLI buffer (20 mM phosphate buffer, 8 mM KCl, 137 mM NaCl, 0.05% surfactant P20) | DNA | 38784467 | 10.1039/d3md00752a | for AS1411, the K d value was 17.5 nM (Fig. 6B) | step2c_acs_v1 | ||||
| 475 | Escherichia coli O157:H7 | protein | E. coli O157:H7-specific aptamer | CCGGACGCTTATGCCTTGCCATCTACAGAGCAGGTGTGACGG | 1.92e-08 M | -7.717 | apparent_cellular | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | fluorescence | 298.15 | liquid milk-based matrices (0% lactalbumin/lactose/casein) | DNA | FAM | 41850902 | 10.1021/acs.analchem.5c07364 | the aptamer exhibited enhanced binding affinity in the crowded microenvironment, with a 25% reduction in Kd (from 19.2 to 14.4 nM). | step2c_acs_v1 | ||||
| 441 | xanthylacrylamide | protein | XAA-1 | GACGACGTAGGTGTGGATGGCTTTGAAAAAGGGCTAGTCGTC | 2e-08 M | -7.699 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | 40261307 | 10.1021/acs.analchem.5c00783 | The true K d of aptamer XAA-1 was calculated to be 20 nM after accounting for the competitive effect of the quencher-labeled strand | step2c_acs_v1 | |||||||||
| 422 | hnRNP A1 | protein | P09651 | TBA | GGTTGGTGTGGTTGG | 2.1100000000000004e-08 M | -7.676 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | BLI | 7.4 | BLI buffer (20 mM phosphate buffer, 8 mM KCl, 137 mM NaCl, 0.05% surfactant P20) | DNA | 38784467 | 10.1039/d3md00752a | for TBA, the K d value was 21.1 nM (Fig. 6A) | step2c_acs_v1 | ||||
| 357 | HBeAg | protein | A-9 | AGCAGCACAGAGGTCAGATGAGGCCTGGTGATCGTGCCCAGGCCATATGAGCAAGGAACCCCTATGCGTGCTACCGTGAA | 2.29e-08 M | -7.64 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | affinity_real_time_qPCR | 7.4 | 1 × BB (50 mM Tris-HCl (pH 7.4), 5 mM KCl, 50 mM NaCl, 7 mM MgCl2, and 0.05% Tween 20) | DNA | 32250595 | 10.1021/acs.analchem.9b05740 | The measured dissociation constant ( K d) is improved by 19 times from a K d value of 22.9 nM with the 80-nt sequence to a K d of 1.2 nM with the new 61-nt aptamer. | step2c_acs_v1 | |||||
| 373 | beta-conglutin | protein | 11-mer | GGTGGGGGTGG | 2.3300000000000003e-08 M | -7.633 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | BLI | 303.15 | 7.4 | PBS, 1.5 mM MgCl2, pH 7.4, 0.1% Tween-20 | DNA | 33498970 | 10.3390/ijms22031150 | A 2:1 heterogenous model was used to fit the data and calculate the binding affinities resulting in two different KD values of 6.95 and 23.30 nM. | step2c_acs_v1 | ||||
| 485 | melamine | protein | Mel36-1 | GGAGTTCGTAGAGGTGTCCTAAGTCTTTAGGTTGGA | 2.4000000000000003e-08 M | -7.62 | non_intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | backfill_text_verified | 298.15 | 42261635 | 10.1021/acs.analchem.6c01553 | Mel36-1 has the most sensitive response with an apparent K d of 24 nM | step2c_acs_v1 | ||||||||
| 317 | Salmonella typhimurium | protein | Q8IWE5 | STYP-3 | GAGTTAATCAATACAAGGCGGGAACATCCTTGGCGGTGC | 2.5000000000000002e-08 M | -7.602 | apparent_cellular | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | 23075417 | 10.1021/ac302902s | It was observed that the aptamer pool collected at the seventh round of selection had the highest binding a ffi nity to the bacteria ( K D = 25 nM). | step2c_acs_v1 | ||||||||
| 416 | Sterigmatocystin | protein | H Seq02 | GAATACGGATTACTGTTCGTACTGACCTATGCTGTGGAGT | 2.53e-08 M | -7.597 | intrinsic | Kd | Gold | v4 | multi_agent_verified | verified_in_text_or_SI | original | ITC | DNA | amino-modified | 38175632 | 10.1021/acs.analchem.3c03675 | The final fitting curve showed a reduced chi-squared (kcal/mol) 2 of 0.871, and the K D value was 25.3 nM. | step2c_acs_v1 |
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CREATE VIEW v_kd AS
SELECT k.id,
target_name_canonical,
CASE
WHEN target_name_canonical LIKE '%cell%' OR target_name_canonical LIKE '%vesicle%' OR target_name_canonical LIKE '%exosome%' THEN 'cell/EV'
WHEN target_name_canonical LIKE '%BSA%' OR target_name_canonical LIKE '%sLe%' OR target_name_canonical LIKE '%glycan%' OR target_name_canonical LIKE '% Le %' THEN 'glycan/conjugate'
ELSE 'protein'
END AS target_type,
target_uniprot, aptamer_name, aptamer_seq,
(COALESCE(kd_value,'') || CASE WHEN COALESCE(kd_unit,'')!='' THEN ' '||kd_unit ELSE '' END) AS kd_reported,
CAST(NULLIF(kd_log10_molar,'') AS REAL) AS kd_log10_molar,
measurement_class, binding_constant_type, 'Gold' AS tier, k.tier AS source_origin,
CASE
WHEN vh.verdict='confirmed' THEN 'human_verified'
WHEN vh.verdict='corrected' THEN 'human_corrected'
WHEN vh.verdict='rejected' THEN 'human_rejected'
WHEN k.verification_status='agent_verified_L2' THEN 'multi_agent_verified'
WHEN k.verification_status IN ('verified','CONFIRM') THEN 'extraction_verified'
ELSE 'automated'
END AS verification_level,
sequence_status, seq_source, pi_provenance_flag,
assay_method,
CAST(NULLIF(assay_temperature_k,'') AS REAL) AS assay_temperature_k,
CAST(NULLIF(assay_ph,'') AS REAL) AS assay_ph,
assay_buffer, assay_cations, aptamer_chemistry, aptamer_modifications,
source_pmid, doi, verbatim_quote, source_db
FROM kd_measurements k LEFT JOIN verification_human vh ON vh.row_id=k.source_record_id
WHERE LOWER(COALESCE(k.include_in_gold,''))='true';