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Enzyme solid-state support assays: a surface plasmon resonance and mass spectrometry coupled study of immobilized insulin degrading enzyme (130 visite)

Grasso G, Bush AI, D'Agata R, Rizzarelli E, Spoto G

Eur Biophys J (ISSN: 1432-1017, 0175-7571), 2009 Apr; 38(4): 407-414.

Tipo di articolo: Journal Article, Research Support, Non-U. S. Gov'T,

Impact factor: 2.437

Impact factor a 5 anni: 2.369


Parole chiave: 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,

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-62949196901&partnerID=40&md5=ec63db6d20956de0ae912ab1bce30385

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.
*** 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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Aguilar, M. -I., Small, D. H., Surface plasmon resonance for the analysis of -amyloid interactions and fibril formation in Alzheimer's disease research (2005) Neurotox Res, 7, pp. 17-2

Andrade, S. M., Carvalho, T. I., Viseu, M. I., Costa, S. M., Conformational changes of beta-lactoglobulin in sodium bis (2-ethylhexyl) sulfosuccinate reverse micelles. A fluorescence and CD study (2004) Eur J Biochem, 271, pp. 734-744. , 10. 1111/j. 1432-1033. 2004. 03977. x

Darnell, J. E., Lodish, H., Baltimore, D., (1990), Scientific American Books New YorkDi Venere, A., Rossi, A., De Matteis, F., Rosato, N., Finazzi Agr, A., Mei, G., Opposite effects of Ca2+ and GTP binding on tissue transglutaminase tertiary structure (2000) J Biol Chem, 275, pp. 3915-3921

Drobny, G. P., Long, J. R., Karlsson, T., Shaw, W., Popham, J., Oyler, N., Bower, P., Stayton, P. S., Structural studies of biomaterials using double-quantum solid-state NMR spectroscopy (2003) Annu Rev Phys Chem, 54, pp. 531-571. , 10. 1146/annurev. physchem. 54. 011002. 103903

Ji, Z. L., Chen, X., Zhen, C. J., Yao, L. X., Han, L. Y., Yeo, W. K., Chung, P. C., Chen, Y. Z., KDBI: Kinetic data of bio-molecular interactions database (2003) Nucleic Acids Res, 31, pp. 255-257. , 10. 1093/nar/gkg067

Jung, L. S., Campbell, C. T., Chinowsky, T. M., Mar, M. N., Yee, S. S., Quantitative interpretation of the response of surface plasmon resonance sensors to adsorbed films (1998) Langmuir, 14, pp. 5636-5648. , 10. 1021/la971228b

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

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Impact factor a 5 anni totale: 85.616 (83.797 escludendo Abstract e Conferenze).







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