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).
25 rows where measurement_class = "intrinsic" and sequence_status = "pending_supp_oa" sorted by kd_log10_molar
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Suggested facets: target_name_canonical, target_uniprot, aptamer_name, kd_reported, kd_log10_molar, source_origin, assay_temperature_k, assay_buffer, source_pmid, doi, verbatim_quote, source_db
assay_method 4
- BLI 9
- ITC 1
- MST 1
- fluorescence 1
verification_level 2
tier 1
- Gold 25
target_type 1
- protein 25
sequence_status 1
- pending_supp_oa · 25 ✖
measurement_class 1
- intrinsic · 25 ✖
binding_constant_type 1
- Kd 25
| 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 |
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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';