SPR and ITC determination of the kinetics and the thermodynamics of bivalent versus monovalent sugar ligand-lectin interactions

Glycoconjugate Journal

Volumn 25, Issue 4, 2008, Pages 313-321

  Murthy, Bandaru Narasimha ^a   Sinha, Sharmistha ^b   Surolia, Avadhesha ^b   Indi, Shantinath S ^a   Jayaraman, Narayanaswamy ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b NATIONAL INSTITUTE OF IMMUNOLOGY   (India)

Author keywords

Dynamic light scattering; Electron microscopy; Isothermal titration calorimetry; Lectins; Sugar ligands; Surface plasmon resonance

Indexed keywords

ALPHA DEXTRO MANNOPYRANOSIDE; LECTIN; LIGAND; SUGAR; UNCLASSIFIED DRUG;

ARTICLE; COMPARATIVE STUDY; COMPLEX FORMATION; CROSS LINKING; DISSOCIATION; ISOTHERMAL TITRATION CALORIMETRY; KINETICS; LIGHT SCATTERING; MORPHOLOGY; PRIORITY JOURNAL; PROTEIN INTERACTION; SOLID STATE; SURFACE PLASMON RESONANCE; THERMODYNAMICS; TRANSMISSION ELECTRON MICROSCOPY;

CALORIMETRY; CARBOHYDRATE CONFORMATION; CARBOHYDRATES; KINETICS; LECTINS; LIGANDS; LIGHT; MICROSCOPY, ELECTRON, TRANSMISSION; SCATTERING, RADIATION; SURFACE PLASMON RESONANCE; THERMODYNAMICS;

EID: 41149135430     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-007-9076-6     Document Type: Article

References (36)

1. Sharon, N., Lis, H.: Lectins as cell recognition molecules. Science 246, 227-234 (1989)
2. Lee, Y.C., Lee, R.T.: Carbohydrate-protein interactions: basics of glycobiology. Acc. Chem. Res. 28, 321-327 (1995)
3. Wong, C.-H.: Carbohydrate-based Drug Discovery, 1st edn. (vols 1 and 2). Wiley-VCH, Weinheim, (2003)
4. Dwek, R.A.: Glycobiology: toward understanding the function of sugars. Chem. Rev. 96, 683-720 (1996)
5. Crocker, P.R., Feizi, T.: Carbohydrate recognition systems: functional triads in cell-cell interactions. Curr. Opin. Struct. Biol. 6, 679-691 (1996)
6. Dam, T.K., Brewer, C.F.: Thermodynamic studies of lectin-carbohydrate interactions by isothermal titration calorimetry. Chem. Rev. 102, 387-430 (2002)
7. Lundquist, J.J., Toone, E.J.: The cluster glycoside effect. Chem. Rev. 102, 555-578 (2002)
8. Mammen, M., Choi, S.-K., Whitesides, G.M.: Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors. Angew. Chem. Int. Ed. 37, 2754-2794 (1998)
9. Monsigny, M., Mayer, R., Roche, A.C.: Sugar-lectin interactions: sugar clusters, lectin multivalency and avidity. Carbohydr. Lett. 4, 35-52 (2000)
10. Kiessling, L.L., Gestwicki, J.E., Strong, L.E.: Synthetic multivalent ligands as probes of signal transduction. Angew. Chem. Int. Ed. 45, 2348-2368 (2006)
11. Fan, E., Zhang, Z., Minke, W.E., Hou, Z., Verlinde, C.L.M.J., Hol, W.G.J.: High-affinity pentavalent ligands of Escherichia coli heat-labile enterotoxin by modular structure-based design. J. Am. Chem. Soc. 122, 2663-2664 (2000)
12. Pavel, I.K., Joanna, M.S., George, M., Glen, D.A., Hong, L., Navraj, S.P., Randy J.R., Bundle, D.R.: Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands. Nature 403, 669-672 (2000)
13. Turnbull, W.B., Kalovidouris, S.A., Stoddart, J.F.: Synthetic carbohydrate dendrimers. Part 9. Large oligosaccharide-based glycodendrimers. Chem. Eur. J. 8, 2988-3000 (2002)
14. Roy, R.: Syntheses and some applications of chemically defined multivalent glycoconjugates. Curr. Opin. Struct. Biol. 6, 692-702 (1996)
15. Reina, J.J., Maldonado, O.S., Tabarani, G., Fieschi, F., Rojo, J.: Mannose glycoconjugates functionalized at positions 1 and 6. Binding analysis to DC-SIGN using biosensors. Bioconjug. Chem. 18, 963-969 (2007)
16. Reiger, J., Stoffelbach, F., Cui, D., Imberty, A., Lameignere, E., Jerome, C., Amely-velty, R.: Mannosylated poly(ethylene oxide)-b-Poly(ε- caprolactone)diblock copolymers: synthesis, characterization, and interaction with a bacterial lectin. Biomacromolecules 8, 2717-2725 (2007)
17. Mangold, S.L., Cloninger, M.J.: Binding of monomeric and dimeric Concanavalin A to mannose-functionalized dendrimers. Org. Biomol. Chem. 4, 2458-2465 (2006)
18. Gestwicki, J.E., Cairo, C.W., Strong, L.E., Oetjen, K.A., Kiessling, L.L.: Influencing receptor-ligand binding mechanisms with multivalent ligand architecture. J. Am. Chem. Soc. 124, 14922-14933 (2002)
19. Dam, T.K., Oscarson, S., Roy, R., Das, S.K., Page, D., Macaluso, F., Brewer, C.F.:Thermodynamic, kinetic, and electron microscopy studies of concanavalin A and Dioclea grandiflora lectin cross-linked with synthetic divalent carbohydrates. J. Biol. Chem. 280, 8640-8646 (2005)
20. Srinivas, O., Mitra, N., Surolia, A., Jayaraman, N.: Photoswitchable multivalent sugar ligands: synthesis, isomerization and lectin binding studies of azobenzene-glycopyranoside conjugates. J. Am. Chem. Soc. 124, 2124-2125 (2002)
21. Srinivas, O., Mitra, N., Surolia, A., Jayaraman, N.: Photoswitchable cluster glycosides as tool to probe carbohydrate-protein interactions: synthesis and lectin-binding studies of azobenzene containing multivalent ligands. Glycobiology 15, 861-873 (2005)
22. Murthy, B.N., Sampath, S., Jayaraman, N.: Synthesis and Langmuir studies of bivalent and monovalent α-D-mannopyranosides with Lectin Con A. Langmuir 21, 9591-9596 (2005)
23. Murthy, B.N., Voelcker, N.H., Jayaraman, N.: Evaluation of α-D-mannopyranoside glycolipids-lectin interactions by surface plasmon resonance methods. Glycobiology 16, 822-832 (2006)
24. Cassel, S., Debig, C., Benvegnu, T., Chaimbault, P., Lafosse, M., Plusquellec, D., Rollin, P.: Original synthesis of linear, branched and cyclic oligoglycerol standards. Eur. J. Org. Chem. 2001, 875-896 (2001)
25. Ness, R.K., Fletcher, Jr H.G., Hudson, C.S.: The reaction of 2,3,4,6-tetrabenzoyl-α-D-glucopyranosyl bromide and 2,3,4,6-tetrabenzoyl- α-D-mannopyranosyl bromide with methanol. Certain benzoylated derivatives of D-Glucose and D-Mannose. J. Am. Chem. Soc. 72, 2200-2205 (1950)
26. Goldstein, I.J., Poretz, R.D.: The Lectins: Properties, Functions and Applications in Biology and Medicine. Academic, New York, pp. 35-244 (1998)
27. Goddard, E.D., Turro, N.J., Kuo, P.L.: Ananthapadmanabhan KP, Fluorescence probes for critical micelle concentration determination. Langmuir 1, 352-355 (1985)
28. Monsigny, M., Frison, N., Duverger, E., Roche, C.A.: Carbohydrate-protein interactions assessed by surface plasmon resonance. Biochemie 85, 167-179 (2003)
29. Surolia, A., Sharma, S., Sikder, B.K., Thomas, J.C., Kapoor, M.: Exploring kinetics and mechanism of protein-sugar recognition by surface plasmon resonance. Methods Enzymol. 362, 312-329 (2003)
30. Gallego, R.E., Haseley, H.R., van Miegem, V.F.L., Vliegenthart, J.F.G., Kamerling, J.P.: Identification of carbohydrates binding to lectins by using surface plasmon resonance in combination with HPLC profiling. Glycobiology 14, 373-386 (2004)
31. Kisseling, L.L., Maly, J.D., Kanai, M., Mann, A.D.: Probing low affinity and multivalent interactions with surface plasmon resonance: ligands for Concanavalin A. J. Am. Chem Soc. 120, 10575-10582 (1998)
32. Myszka, D.G., Hansely, P., Simons, S.P., Lemotte, P.K., Brown, T.A., Geoghegan K.F., Hoth, L.S., Rich, R.L.B.: Kinetic analysis of estrogen receptor/ligand interactions. Proc. Natl. Acad. Sci. USA 99, 8562-8567 (2002)
33. Nagata, Y., Burger, M.M.: Wheat germ agglutinin: molecular characteristics and specificity for sugar binding. J. Biol. Chem. 249, 3116-3122 (1973)
34. An alternate protocol of the ligand immobilization onto the sensor surface was attempted. Thus, ligand 7 was self-assembled into an alkyl thiol functionalized HPA surface. The lectin was introduced as the analyte and an increase in the SPR response, corresponding to the lectin binding onto the ligand-immobilized surface, was observed. However, the subsequent dissociation phase and the regeneration of the sensor surface devoid of the lectin led to drastic decreases in the response units, denoting the loss of the ligand also from the surface during the dissociation and surface regeneration steps. In the light of the loss of the immobilized ligand after the de-complexation, this alternate effort could not be continued further
35. Berne, B.J., Pecora, R.: Dynamic Light Scattering. Wiley, New York (1976)
36. Parkin, S., Rupp, B., Hope, H.: Atomic resolution structure of Con A at 120 K, Acta Cryst D52, 1161-1168 (1996)