Enzyme solid-state support assays: a surface plasmon resonance and mass spectrometry coupled study of immobilized insulin degrading enzyme(601 views) Grasso G, Bush AI, D'Agata R, Rizzarelli E, Spoto G
Keywords: Conformational Change, Insulin Degrading Enzyme, Mass Spectrometry, Solid-State Assay, Surface Plasmon Resonance, Animals, Atmospheric Pressure, Cattle, Immobilized, Gold, Insulysin, Kinetics, Microfluidics, Protein Binding, Protein Conformation, Matrix-Assisted Laser Desorption-Ionization, Spodoptera,
Affiliations: *** IBB - CNR ***
Dipartimento Scienze Chimiche, Universita di Catania, v.le A. Doria 6, 95125, Catania, Italy. grassog@unict.it
Department of Psychiatry, Massachusetts General Hospital, Charlestone, MA, United States
Department of Pathology, Mental Health Research Institute of Victoria, University of Melbourne, Parkville, Australia
Istituto di Biostrutture e Bioimmagini, CNR, v.le A. Doria 6, 95125 Catania, Italy
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Kim, M., Jung, S. O., Park, K., Jeong, E. -J., Joung, H. -A., Kim, T. -H., Seol, D. -W., Chung, B. H., Detection of bax protein conformational change using a surface plasmon resonance imaging-based antibody chip (2005) Biochem Biophys Res Commun, 338, pp. 1834-1838. , 10. 1016/j. bbrc. 2005. 10. 155
Kurochkin, I. V., Goto, S., Alzheimer's -amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme (1994) FEBS Lett, 345, pp. 33-37. , 10. 1016/0014-5793 (94) 00387-4
Leissring, M. A., Selkoe, D. J., Structural biology: Enzyme target to latch on to (2006) Nature, 443, pp. 761-762. , 10. 1038/nature05210
Leslie, T. E., Lilley, T. H., Aqueous solutions containing amino acids and peptides. Part 20. Volumetric behavior of some terminally substituted amino acids and peptides at 298. 15 K (1985) Biopolymers, 24, pp. 695-710. , 10. 1002/bip. 360240409
Miners, J. S., Kehoe, P. G., Love, S., Immunocapture-based fluorometric assay for the measurement of insulin-degrading enzyme activity in brain tissue homogenates (2008) J Neurosci Methods, 169, pp. 177-181. , 10. 1016/j. jneumeth. 2007. 12. 003
Myszka, D. G., Morton, T. A., CLAMP: A biosensor kinetic data analysis program (1998) Trends Biochem Sci, 23, pp. 149-150. , 10. 1016/S0968-0004 (98) 01183-9
Myszka, D. G., Wood, S. J., Biere, A. L., Analysis of fibril elongation using surface plasmon resonance biosensors (1999) Methods Enzymol, 309, pp. 386-402. , 10. 1016/S0076-6879 (99) 09027-8
Sharff, A. J., Rodseth, L. E., Spurlino, J. C., Quiocho, F. A., Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis (1992) Biochemistry, 31, pp. 10657-10663. , 10. 1021/bi00159a003
Song, E. S., Juliano, M. A., Juliano, L., Hersh, L. B., Substrate activation of insulin degrading enzyme (insulysin), a potential target for drug development (2003) J Biol Chem, 278, pp. 49789-49794. , 10. 1074/jbc. M308983200
Veps l inen, S., Parkinson, M., Helisalmi, S., Mannermaa, A., Soininen, H., Tanzi, R. E., Bertram, L., Hiltunen, M., Insulin-degrading enzyme is genetically associated with Alzheimer's disease in the Finnish population (2007) J Med Genet, 44, pp. 606-608. , 10. 1136/jmg. 2006. 048470
Yowler, B. C., Schengrund, C. -L., Botulinum neurotoxin A changes conformation upon binding to ganglioside GT1b (2004) Biochemistry, 43, pp. 9725-9731. , 10. 1021/bi0494673
Enzyme solid-state support assays: a surface plasmon resonance and mass spectrometry coupled study of immobilized insulin degrading enzyme
Solid-support based assays offer several advantages that are not normally available in solution. Enzymes that are anchored on gold surfaces can interact with several different molecules, opening the way to high throughput array format based assays. In this scenario, surface plasmon resonance (SPR) and mass spectrometry (MS) investigations have often been applied to analyze the interaction between immobilized enzyme and its substrate molecules in a tag-free environment. Here, we propose a SPR-MS combined experimental approach aimed at studying insulin degrading enzyme (IDE) immobilized onto gold surfaces and its ability to interact with insulin. The latter is delivered by a microfluidic system to the IDE functionalized surface and the activity of the immobilized enzyme is verified by atmospheric pressure/matrix assisted laser desorption ionization (AP/MALDI) MS analysis. The SPR experiments allow the calculation of the kinetic constants involved for the interaction between immobilized IDE and insulin molecules and evidence of IDE conformational change upon insulin binding is also obtained.
Enzyme solid-state support assays: a surface plasmon resonance and mass spectrometry coupled study of immobilized insulin degrading enzyme