Amyloid beta 25-35 [A beta (25-35)], as a peptide model for full-Length A beta in structural and functional investigations, has been chosen for aggregation studies. The complexity of the A beta (25-35) aggregation process required a multi-methodological analytical approach to obtain reliable and reproducible results. Here, we describe the results obtained by the use of mass spectrometry (MS) for the structural characterization of the self-assembly species during the aggregation process and for the definition of the self-assembly kinetics and myricetin inhibition patterns, comparing the results with those obtained by using the well-established spectroscopic method based on thioflavin T fluorescence. Flow injection electrospray ionization-ion trap-mass spectrometry (ESI-IT-MS) was applied to monitor the disappearance of the monomer specie in the first steps, whereas matrix-assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-ToF-MS) was used to follow monomer and small oligomer self-assembly trends in the early stages of the nucleating process.
Mass Spectrometry as efficient tool for the characterization of amyloid peptide 25-35 self-assembly species in aggregation and inhibition studies / J. Fiori; M. Naldi; V. Andrisano. - In: EUROPEAN JOURNAL OF MASS SPECTROMETRY. - ISSN 1469-0667. - STAMPA. - 19:6(2013), pp. 483-490. [10.1255/ejms.1255]
Mass Spectrometry as efficient tool for the characterization of amyloid peptide 25-35 self-assembly species in aggregation and inhibition studies
FIORI, JESSICA;NALDI, MARINA;ANDRISANO, VINCENZA
2013
Abstract
Amyloid beta 25-35 [A beta (25-35)], as a peptide model for full-Length A beta in structural and functional investigations, has been chosen for aggregation studies. The complexity of the A beta (25-35) aggregation process required a multi-methodological analytical approach to obtain reliable and reproducible results. Here, we describe the results obtained by the use of mass spectrometry (MS) for the structural characterization of the self-assembly species during the aggregation process and for the definition of the self-assembly kinetics and myricetin inhibition patterns, comparing the results with those obtained by using the well-established spectroscopic method based on thioflavin T fluorescence. Flow injection electrospray ionization-ion trap-mass spectrometry (ESI-IT-MS) was applied to monitor the disappearance of the monomer specie in the first steps, whereas matrix-assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-ToF-MS) was used to follow monomer and small oligomer self-assembly trends in the early stages of the nucleating process.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.