Maldi, Ap/Maldi And Esi Techniques For The Ms Detection Of Amyloid Beta-Peptides
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Maldi, Ap/Maldi And Esi Techniques For The Ms Detection Of Amyloid Beta-Peptides (343 views visite)

Grasso G, Mineo P, Rizzarelli E, Spoto G

Int J Mass Spectrom (ISSN: 1387-3806), 2009 Apr 15; 282(1-2): 50-55.



Paper type Tipo di articolo: Journal Article,

Impact factor: 2.117, 5-year impact factor Impact factor a 5 anni: 2.304

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-62849088434&partnerID=40&md5=09bac6b3b2d72966923887abe0884156

Keywords Parole chiave: Amyloid Peptide, Fragmentation, Maldi, Matrix,

Affiliations Affiliazioni:

*** IBB - CNR ***
Chemistry Department, Università di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Istituto Biostrutture e Bioimmagini, CNR, Viale A. Doria 6, Catania, Italy


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Hamley, I.W., (2007) Angew. Chem. Int. Ed., 46, p. 8128

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Butterfield, D. A., Reed, T., Newman, S. F., Sultana, R., (2007) Free Radic. Biol. Med., 43, p. 65

Selkoe, D. J., (1994) J. Neuropathol. Exp. Neurol., 53, p. 438

Hamley, I. W., (2007) Angew. Chem. Int. Ed., 46, p. 8128

Nilsson, K. P., Hammarstroem, P., Ahlgren, F., Herland, A., Schnell, E. A., Lindgren, M., Westermark, G. T., Inganaes, O., (2006) ChemBioChem, 7, p. 1096

Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Klein, W. L., (1998) Proc. Natl. Acad. Sci., 95, p. 6448

Turner, A. J., Fisk, L., Nalivaeva, N. N., (2004) Ann. N. Y. Acad. Sci., 1035, p. 1

Eckman, E. A., Eckman, C. B., (2005) Biochem. Soc. Trans., 33, p. 1101

Luchsinger, J. A., Tang, M. X., Shea, S., Mayeux, R., (2004) Neurology, 63, p. 1187

Qiu, W. Q., Folstein, M. F., (2006) Neurobiol. Aging, 27, p. 190

Kurochkin, I. V., Goto, S., (1994) FEBS Lett., 345, p. 33

Leissring, M. A., Lu, A., Condron, M. M., Teplow, D. B., Stein, R. L., Farris, W., Selkoe, D. J., (2003) J. Biol. Chem., 278, p. 37314

Shen, C. -L., Murphy, R. M., (1995) Biophys. J., 69, p. 640

Chen, M., Cook, K. D., (2007) Anal. Chem., 79, p. 2031

Klug, G. M. J. A., Losic, D., Subasinghe, S. S., Aguilar, M. -I., Martin, L. L., Small, D. H., (2003) Eur. J. Biochem., 270, p. 4282

Taylor, B. M., Sarver, R. W., Fici, G., Poorman, R. A., Lutzke, B. S., Molinari, A., Kawabe, T., Epps, D. E., (2003) J. Protein Chem., 22, p. 31

Snyder, S. W., Ladror, U. S., Wade, W. S., Wang, G. T., Barrett, L. W., Matayoshi, E. D., Huffaker, H. J., Holzman, T. F., (1994) Biophys. J., 67, p. 1216

Sabat, R., Gallardo, M., Estelrich, J., (2005) Int. J. Biol. Macromol., 35, p. 9

Tan, P. V., Laiko, V. V., Doroshenko, V. M., (2004) Anal. Chem., 75, p. 2462

Smith, A. M., Jahn, T. R., Ashcroft, A. E., Radford, S. E., (2006) J. Mol. Biol., 364, p. 9

Caddy, G. L., Robinson, C. V., (2006) Protein Peptide Lett., 13, p. 255

Mehl, J. T., Cummings, J. J., Rohde, E., Yates, N. N., (2003) Rapid Commun. Mass Spectrom., 17, p. 1600

Konn, D. O., Murrell, J., Despeyroux, D., Gaskell, S. J., (2005) J. Am. Soc. Mass Spectrom., 16, p. 743

Cohen, S. L., Chait, B. T., (1996) Anal. Chem., 68, p. 31

Nikogosyan, D. N., G rner, H., (1999) IEEE J. Sel. Top. Quant. Electronics, 5, p. 1107

Brown, R. S., Feng, J., Reiber, D. C., (1997) Int. J. Ion Process. Mass Spectrom., 169-170, p. 1

Petre, B. -A., Youhnovski, N., Lukkari, J., Weber, R., Przybylski, M., (2005) Eur. J. Mass Spectrom., 11, p. 513

Wang, D. -S., Dickson, D. W., Malter, J. S., (2006) J. Biomed. Biotechnol. ID, 58406, p. 1

Song, E. -S., Mukherjee, A., Juliano, M. A., St Pyrek, J., Goodman, J. P., Juliano Jr., L., Hersh, L. B., (2001) J. Biol. Chem., 276, p. 1152

Zagorski, M. G., Yang, J., Shao, H., Ma, K., Zeng, H., Hong, A., (1999) Methods Enzymol., 309, p. 189



Amyloid β-peptides (Aβs) are involved in several neuropathological conditions such as Alzheimer's disease and considerable experimental evidences have emerged indicating that different proteases play a major role in regulating the accumulation of Aβs in the brain. Particularly, insulin-degrading enzyme (IDE) has been shown to degrade Aβs at different cleavage sites, but the experimental results reported in the literature and obtained by mass spectrometry methods are somehow fragmentary. The detection of Aβs is often complicated by solubility issues, oxidation artifacts and spontaneous aggregation/cleavage and, in order to rationalize the different reported results, we analyzed Aβs solutions by three different MS approaches: matrix assisted laser desorption ionization-time of flight (MALDI-TOF), atmospheric pressure (AP) MALDI ion trap and electrospray ionization (ESI) ion trap. Differences in the obtained results are discussed and ESI is chosen as the most suitable MS method for Aβs detection. Finally, cleavage sites produced by interaction of Aβs with IDE are identified, two of which had never been reported in the literature. © 2009 Elsevier B.V. All rights reserved.
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8 Records (7 escludendo Abstract e Conferenze).
Impact factor totale: 28.037 (28.037 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 22.632 (22.632 escludendo Abstract e Conferenze).







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