Glyco Property List
Pooled literature properties (glycanDB). Optional filters: ?dataset=uv_vis&property_key=...
GET /api/gdd/glyco-properties/?format=api
{ "count": 839, "next": "http://glycodata.org/api/gdd/glyco-properties/?format=api&page=2", "previous": null, "results": [ { "id": 1, "dataset": "carbohydrate", "entity": "methyl alpha-D-mannopyranoside", "entity_group": "", "entity_class": "glycoside", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "122", "unit": "µM", "value_reported": "122", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs Concanavalin A, isothermal titration calorimetry (ITC), value from Mandal, Kishore & Brewer (Biochemistry 1994, 33:1149-1156); Ka = 0.82 x 10^4 M^-1", "conditions": "Kd vs Concanavalin A, isothermal titration calorimetry (ITC), value from Mandal, Kishore & Brewer (Biochemistry 1994, 33:1149-1156); Ka = 0.82 x 10^4 M^-1", "conditions_detail": "Kd vs Concanavalin A, isothermal titration calorimetry (ITC), value from Mandal, Kishore & Brewer (Biochemistry 1994, 33:1149-1156); Ka = 0.82 x 10^4 M^-1 | partner: Concanavalin A | technique: ITC", "doi": "10.1016/j.jelechem.2016.09.045", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC5388449/", "year": "2016", "confidence": "high", "comments": "\"The Ka value for methyl alpha-D-mannopyranoside reported in the study was 0.82 x 10^4 (Kd = 122 microM)\" — Kd value originally from Mandal, Kishore & Brewer 1994 (DOI 10.1021/bi00171a014), quoted in this paper. Monosaccharide, monovalent ITC affinity. [Bhattarai JK, Tan YH, Pandey B, Fujikawa K, Demchenko AV, Stine KJ, 2016, confidence: high]" }, { "id": 2, "dataset": "carbohydrate", "entity": "monomannoside (Man-C8-SH self-assembled monolayer)", "entity_group": "", "entity_class": "monosaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "0.07", "unit": "µM", "value_reported": "70", "unit_reported": "nM", "method": "Experiment", "method_detail": "Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated mannoside SAM on gold; reported 70 +/- 19 nM", "conditions": "Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated mannoside SAM on gold; reported 70 +/- 19 nM", "conditions_detail": "Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated mannoside SAM on gold; reported 70 +/- 19 nM | partner: Concanavalin A | technique: electrochemical impedance spectroscopy", "doi": "10.1016/j.jelechem.2016.09.045", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC5388449/", "year": "2016", "confidence": "high", "comments": "\"Man(1-3)Man-C8-SH ... show the comparable Kd of 70 +/- 19, 75 +/- 20 and 81 +/- 31 nM\" — Surface-immobilized mannoside (multivalent/avidity context), measured by EIS. [Bhattarai JK, Tan YH, Pandey B, Fujikawa K, Demchenko AV, Stine KJ, 2016, confidence: high]" }, { "id": 3, "dataset": "carbohydrate", "entity": "alpha(1-6)-linked dimannoside (Man(1-6)Man-C8-SH SAM)", "entity_group": "", "entity_class": "disaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "0.014", "unit": "µM", "value_reported": "14", "unit_reported": "nM", "method": "Experiment", "method_detail": "Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated dimannoside SAM on gold; reported 14 +/- 4 nM", "conditions": "Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated dimannoside SAM on gold; reported 14 +/- 4 nM", "conditions_detail": "Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated dimannoside SAM on gold; reported 14 +/- 4 nM | partner: Concanavalin A | technique: electrochemical impedance spectroscopy", "doi": "10.1016/j.jelechem.2016.09.045", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC5388449/", "year": "2016", "confidence": "high", "comments": "\"Man(1-6) Man-C8-SH ... show stronger interaction with Con A with Kd of 14 +/- 4 and 30 +/- 5 nM\" — Surface-immobilized dimannoside, EIS. [Bhattarai JK, Tan YH, Pandey B, Fujikawa K, Demchenko AV, Stine KJ, 2016, confidence: high]" }, { "id": 4, "dataset": "carbohydrate", "entity": "alpha(1-3,1-6) trimannoside (Man(1-3,1-6)Man-C8-SH SAM)", "entity_group": "", "entity_class": "oligosaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "0.03", "unit": "µM", "value_reported": "30", "unit_reported": "nM", "method": "Experiment", "method_detail": "Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated trimannoside SAM on gold; reported 30 +/- 5 nM", "conditions": "Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated trimannoside SAM on gold; reported 30 +/- 5 nM", "conditions_detail": "Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated trimannoside SAM on gold; reported 30 +/- 5 nM | partner: Concanavalin A | technique: electrochemical impedance spectroscopy", "doi": "10.1016/j.jelechem.2016.09.045", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC5388449/", "year": "2016", "confidence": "high", "comments": "\"Man(1-3,1-6)Man-C8-SH show stronger interaction with Con A with Kd of 14 +/- 4 and 30 +/- 5 nM\" — Surface-immobilized core trimannoside, EIS. [Bhattarai JK, Tan YH, Pandey B, Fujikawa K, Demchenko AV, Stine KJ, 2016, confidence: high]" }, { "id": 5, "dataset": "carbohydrate", "entity": "core trimannoside (methyl 3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside)", "entity_group": "", "entity_class": "oligosaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "2", "unit": "µM", "value_reported": "2.0", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs Concanavalin A, isothermal titration calorimetry (ITC); O-methylated alpha(1-3,1-6) trimannoside, Ka = 4.90 x 10^5 M^-1 (Mandal & Brewer)", "conditions": "Kd vs Concanavalin A, isothermal titration calorimetry (ITC); O-methylated alpha(1-3,1-6) trimannoside, Ka = 4.90 x 10^5 M^-1 (Mandal & Brewer)", "conditions_detail": "Kd vs Concanavalin A, isothermal titration calorimetry (ITC); O-methylated alpha(1-3,1-6) trimannoside, Ka = 4.90 x 10^5 M^-1 (Mandal & Brewer) | partner: Concanavalin A | technique: ITC", "doi": "10.1021/bi00171a014", "source_url": "https://pubmed.ncbi.nlm.nih.gov/8110746/", "year": "1994", "confidence": "medium", "comments": "\"For the O-methylated alpha(1-3,1-6) trimannoside, Ka = 4.90 x 10^5 (Kd = 2.0 microM) was reported, while the O-methylated alpha(1-6)-linked dimannoside showed Ka = 0.81 x 10^4 (Kd = 123 microM)\" — Core trimannoside is the conserved binding unit of N-linked glycans; ~60-fold higher affinity than methyl mannoside per Mandal & Brewer 1994. Value via search aggregation of the primary ITC paper. [Mandal DK, Kishore N, Brewer CF, 1994, confidence: medium]" }, { "id": 6, "dataset": "carbohydrate", "entity": "alpha(1-6)-linked dimannoside (O-methylated)", "entity_group": "", "entity_class": "disaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "123", "unit": "µM", "value_reported": "123", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs Concanavalin A, isothermal titration calorimetry (ITC); Ka = 0.81 x 10^4 M^-1 (Mandal & Brewer)", "conditions": "Kd vs Concanavalin A, isothermal titration calorimetry (ITC); Ka = 0.81 x 10^4 M^-1 (Mandal & Brewer)", "conditions_detail": "Kd vs Concanavalin A, isothermal titration calorimetry (ITC); Ka = 0.81 x 10^4 M^-1 (Mandal & Brewer) | partner: Concanavalin A | technique: ITC", "doi": "10.1021/bi00171a014", "source_url": "https://pubmed.ncbi.nlm.nih.gov/8110746/", "year": "1994", "confidence": "medium", "comments": "\"the O-methylated alpha(1-6)-linked dimannoside showed Ka = 0.81 x 10^4 (Kd = 123 microM)\" — Value via search aggregation of the primary ITC paper. [Mandal DK, Kishore N, Brewer CF, 1994, confidence: medium]" }, { "id": 7, "dataset": "carbohydrate", "entity": "lactose", "entity_group": "", "entity_class": "disaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "89.7", "unit": "µM", "value_reported": "89.7", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 89.7 +/- 15.8 uM (TFS) / 93.5 +/- 9.1 uM by ITC, 25 C, PBS", "conditions": "Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 89.7 +/- 15.8 uM (TFS) / 93.5 +/- 9.1 uM by ITC, 25 C, PBS", "conditions_detail": "Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 89.7 +/- 15.8 uM (TFS) / 93.5 +/- 9.1 uM by ITC, 25 C, PBS | partner: galectin-3 | technique: intrinsic tryptophan fluorescence | temperature C: 25", "doi": "10.1038/s41598-019-47658-8", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/", "year": "2019", "confidence": "high", "comments": "\"followed by lactose (KD, 89.7 +/- 15.8 microM)\" — Cross-validated with ITC (93.5 +/- 9.1 uM) in same study. [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]" }, { "id": 8, "dataset": "carbohydrate", "entity": "N-acetyllactosamine (LacNAc)", "entity_group": "", "entity_class": "disaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "27.9", "unit": "µM", "value_reported": "27.9", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 27.9 +/- 4.6 uM (TFS) / 24.0 +/- 3.6 uM by ITC, 25 C, PBS", "conditions": "Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 27.9 +/- 4.6 uM (TFS) / 24.0 +/- 3.6 uM by ITC, 25 C, PBS", "conditions_detail": "Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 27.9 +/- 4.6 uM (TFS) / 24.0 +/- 3.6 uM by ITC, 25 C, PBS | partner: galectin-3 | technique: intrinsic tryptophan fluorescence | temperature C: 25", "doi": "10.1038/s41598-019-47658-8", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/", "year": "2019", "confidence": "high", "comments": "\"LacNAc emerged as the strongest galectin-3 binding ligand (KD, 27.9 +/- 4.6 microM)\" — Cross-validated with ITC (24.0 +/- 3.6 uM). [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]" }, { "id": 9, "dataset": "carbohydrate", "entity": "galactose", "entity_group": "", "entity_class": "monosaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "4700", "unit": "µM", "value_reported": "4.7", "unit_reported": "mM", "method": "Experiment", "method_detail": "Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 4.7 +/- 0.3 mM (TFS) / 3.1 +/- 1.1 mM by ITC, 25 C, PBS", "conditions": "Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 4.7 +/- 0.3 mM (TFS) / 3.1 +/- 1.1 mM by ITC, 25 C, PBS", "conditions_detail": "Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 4.7 +/- 0.3 mM (TFS) / 3.1 +/- 1.1 mM by ITC, 25 C, PBS | partner: galectin-3 | technique: intrinsic tryptophan fluorescence | temperature C: 25", "doi": "10.1038/s41598-019-47658-8", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/", "year": "2019", "confidence": "high", "comments": "\"and galactose (KD, 4.7 +/- 0.3 mM)\" — Monosaccharide weak binding; cross-validated with ITC (3.1 +/- 1.1 mM). [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]" }, { "id": 10, "dataset": "carbohydrate", "entity": "N-acetyllactosamine (LacNAc)", "entity_group": "", "entity_class": "disaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "654.4", "unit": "µM", "value_reported": "654.4", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs human galectin-2, intrinsic tryptophan fluorescence spectroscopy (TFS); 654.4 +/- 155.4 uM (TFS) / 554.2 +/- 108.0 uM by ITC, 25 C, PBS", "conditions": "Kd vs human galectin-2, intrinsic tryptophan fluorescence spectroscopy (TFS); 654.4 +/- 155.4 uM (TFS) / 554.2 +/- 108.0 uM by ITC, 25 C, PBS", "conditions_detail": "Kd vs human galectin-2, intrinsic tryptophan fluorescence spectroscopy (TFS); 654.4 +/- 155.4 uM (TFS) / 554.2 +/- 108.0 uM by ITC, 25 C, PBS | partner: galectin-2 | technique: intrinsic tryptophan fluorescence | temperature C: 25", "doi": "10.1038/s41598-019-47658-8", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/", "year": "2019", "confidence": "high", "comments": "\"The KD values of LacNAc, lactose and galactose binding to galectin-2 were 654.4 +/- 155.4 microM\" — Cross-validated with ITC (554.2 +/- 108.0 uM). [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]" }, { "id": 11, "dataset": "carbohydrate", "entity": "lactose", "entity_group": "", "entity_class": "disaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "589.3", "unit": "µM", "value_reported": "589.3", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs human galectin-4 (full-length), intrinsic tryptophan fluorescence spectroscopy (TFS); 589.3 +/- 168.2 uM (TFS) / 738.5 +/- 128.5 uM by ITC, 25 C, PBS", "conditions": "Kd vs human galectin-4 (full-length), intrinsic tryptophan fluorescence spectroscopy (TFS); 589.3 +/- 168.2 uM (TFS) / 738.5 +/- 128.5 uM by ITC, 25 C, PBS", "conditions_detail": "Kd vs human galectin-4 (full-length), intrinsic tryptophan fluorescence spectroscopy (TFS); 589.3 +/- 168.2 uM (TFS) / 738.5 +/- 128.5 uM by ITC, 25 C, PBS | partner: galectin-4 | technique: intrinsic tryptophan fluorescence | temperature C: 25", "doi": "10.1038/s41598-019-47658-8", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/", "year": "2019", "confidence": "high", "comments": "\"The binding of galectin-4 to lactose (KD, 589.3 +/- 168.2 microM) was stronger than to LacNAc\" — Cross-validated with ITC (738.5 +/- 128.5 uM). Galectin-4 binds lactose more strongly than LacNAc (unusual). [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]" }, { "id": 12, "dataset": "carbohydrate", "entity": "lactose", "entity_group": "", "entity_class": "disaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "230", "unit": "µM", "value_reported": "230", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs galectin-3 carbohydrate recognition domain (Gal3C), ITC and NMR, room temperature", "conditions": "Kd vs galectin-3 carbohydrate recognition domain (Gal3C), ITC and NMR, room temperature", "conditions_detail": "Kd vs galectin-3 carbohydrate recognition domain (Gal3C), ITC and NMR, room temperature | partner: galectin-3 (Gal3C CRD) | technique: ITC/NMR", "doi": "10.1021/bi201459p", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC3255464/", "year": "2011", "confidence": "high", "comments": "\"lactose binds to Gal3C with a dissociation constant (Kd) of 230 microM\" — Same paper also notes 3'-benzamido-LacNAc Kd = 18.2 uM and lactose Kd = 231 uM. [Saraboji K, Hakansson M, Genheden S, et al., 2011, confidence: high]" }, { "id": 13, "dataset": "carbohydrate", "entity": "3'-benzamido-N-acetyllactosamine", "entity_group": "", "entity_class": "glycoside", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "18.2", "unit": "µM", "value_reported": "18.2", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs galectin-3 carbohydrate recognition domain (Gal3C), referenced value, room temperature", "conditions": "Kd vs galectin-3 carbohydrate recognition domain (Gal3C), referenced value, room temperature", "conditions_detail": "Kd vs galectin-3 carbohydrate recognition domain (Gal3C), referenced value, room temperature | partner: galectin-3 (Gal3C CRD) | technique: ITC", "doi": "10.1021/bi201459p", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC3255464/", "year": "2011", "confidence": "high", "comments": "\"affinity of lactose is lower (Kd = 231 microM) than that of 3'-benzamido-N-acetyllactosamine (Kd = 18.2 microM)\" — Synthetic high-affinity galectin-3 ligand. [Saraboji K, Hakansson M, Genheden S, et al., 2011, confidence: high]" }, { "id": 14, "dataset": "carbohydrate", "entity": "single N-glycans", "entity_group": "", "entity_class": "glycan (N-linked)", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "50", "unit": "µM", "value_reported": "50", "unit_reported": "uM", "method": "Experiment", "method_detail": "Approximate Kd vs galectin-1 CRD for single N-glycans (comparison statement)", "conditions": "Approximate Kd vs galectin-1 CRD for single N-glycans (comparison statement)", "conditions_detail": "Approximate Kd vs galectin-1 CRD for single N-glycans (comparison statement) | partner: galectin-1 | technique: fluorescence anisotropy / comparison", "doi": "10.1093/glycob/cwn015", "source_url": "https://academic.oup.com/glycob/article/18/5/384/1987867", "year": "2008", "confidence": "medium", "comments": "\"The galectin-1 CRDs bind more weakly to single N-glycans (Kd ~50 microM) compared to galectin-3\" — Approximate value (~50 uM). [Cederfur C, Salomonsson E, Nilsson J, et al., 2008, confidence: medium]" }, { "id": 15, "dataset": "carbohydrate", "entity": "human serum glycoproteins (LacNAc-bearing)", "entity_group": "", "entity_class": "glycan (N-linked)", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "3", "unit": "µM", "value_reported": "3", "unit_reported": "uM", "method": "Experiment", "method_detail": "Average Kd vs galectin-3, fluorescence anisotropy assay; estimated range 1-5 uM (midpoint 3 uM recorded)", "conditions": "Average Kd vs galectin-3, fluorescence anisotropy assay; estimated range 1-5 uM (midpoint 3 uM recorded)", "conditions_detail": "Average Kd vs galectin-3, fluorescence anisotropy assay; estimated range 1-5 uM (midpoint 3 uM recorded) | partner: galectin-3 | technique: fluorescence anisotropy", "doi": "10.1093/glycob/cwn015", "source_url": "https://academic.oup.com/glycob/article/18/5/384/1987867", "year": "2008", "confidence": "medium", "comments": "\"The average affinity of galectin-3 for serum glycoproteins was estimated to correspond to Kd ~1-5 microM\" — Reported as a range 1-5 uM; midpoint 3 uM recorded for value field. Glycoprotein-level (multivalent) average affinity. [Cederfur C, Salomonsson E, Nilsson J, et al., 2008, confidence: medium]" }, { "id": 16, "dataset": "carbohydrate", "entity": "L-fucose", "entity_group": "", "entity_class": "monosaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "2.9", "unit": "µM", "value_reported": "2.9", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC)", "conditions": "Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC)", "conditions_detail": "Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC) | partner: LecB (PA-IIL), Pseudomonas aeruginosa | technique: ITC", "doi": "10.32607/20758251-2015-7-2-29-41", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC4463410/", "year": "2015", "confidence": "high", "comments": "\"The dissociation constant of the LecB-L-fucose complex is 2.9 microM\" — Unusually high monosaccharide affinity due to two calcium ions in the LecB binding site. [Grishin AV, Krivozubov MS, Karyagina AS, Gintsburg AL, 2015, confidence: high]" }, { "id": 17, "dataset": "carbohydrate", "entity": "methyl-alpha-L-fucoside", "entity_group": "", "entity_class": "glycoside", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "0.4", "unit": "µM", "value_reported": "0.4", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC; ~7-fold lower than free L-fucose", "conditions": "Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC; ~7-fold lower than free L-fucose", "conditions_detail": "Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC; ~7-fold lower than free L-fucose | partner: LecB (PA-IIL), Pseudomonas aeruginosa | technique: ITC", "doi": "10.32607/20758251-2015-7-2-29-41", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC4463410/", "year": "2015", "confidence": "high", "comments": "\"the dissociation constant of the LecB-methyl-alpha-L-fucoside complex is sevenfold lower than that of the LecB complex with unmodified L-fucose\" — ~0.4 uM (sevenfold below the 2.9 uM fucose value). [Grishin AV, Krivozubov MS, Karyagina AS, Gintsburg AL, 2015, confidence: high]" }, { "id": 18, "dataset": "carbohydrate", "entity": "Lewis a oligosaccharide", "entity_group": "", "entity_class": "oligosaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "0.2", "unit": "µM", "value_reported": "0.2", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC (210 nM); 0.51 uM by ELLA", "conditions": "Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC (210 nM); 0.51 uM by ELLA", "conditions_detail": "Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC (210 nM); 0.51 uM by ELLA | partner: LecB (PA-IIL), Pseudomonas aeruginosa | technique: ITC", "doi": "10.32607/20758251-2015-7-2-29-41", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC4463410/", "year": "2015", "confidence": "high", "comments": "\"The Kd of the LecB-Lea complex is 210 nM\" — Lewis a is a natural fucosylated epitope; recorded as 0.2 uM (210 nM). [Grishin AV, Krivozubov MS, Karyagina AS, Gintsburg AL, 2015, confidence: high]" }, { "id": 19, "dataset": "carbohydrate", "entity": "galactose", "entity_group": "", "entity_class": "monosaccharide", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "88", "unit": "µM", "value_reported": "88", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC)", "conditions": "Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC)", "conditions_detail": "Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC) | partner: LecA (PA-IL), Pseudomonas aeruginosa | technique: ITC", "doi": "10.32607/20758251-2015-7-2-29-41", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC4463410/", "year": "2015", "confidence": "high", "comments": "\"The dissociation constant of the LecA-galactose complex is 88 microM\" — LecA (PA-IL) is the galactose-specific lectin of P. aeruginosa. [Grishin AV, Krivozubov MS, Karyagina AS, Gintsburg AL, 2015, confidence: high]" }, { "id": 20, "dataset": "carbohydrate", "entity": "p-nitrophenyl alpha-D-galactopyranoside", "entity_group": "", "entity_class": "glycoside", "property": "protein binding affinity (Kd)", "property_key": "binding_affinity", "value": "14.1", "unit": "µM", "value_reported": "14.1", "unit_reported": "uM", "method": "Experiment", "method_detail": "Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, ITC; reported within 4-15 uM range for aryl galactosides", "conditions": "Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, ITC; reported within 4-15 uM range for aryl galactosides", "conditions_detail": "Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, ITC; reported within 4-15 uM range for aryl galactosides | partner: LecA (PA-IL), Pseudomonas aeruginosa | technique: ITC", "doi": "10.32607/20758251-2015-7-2-29-41", "source_url": "https://pmc.ncbi.nlm.nih.gov/articles/PMC4463410/", "year": "2015", "confidence": "medium", "comments": "\"Kd of the complex between LecA and such compounds as phenylgalactopyranoside, p-nitrophenylgalactopyranoside ... is 4-15 microM\" — Aromatic aglycone enhances affinity over galactose; value within stated 4-15 uM range. [Grishin AV, Krivozubov MS, Karyagina AS, Gintsburg AL, 2015, confidence: medium]" } ] }