Following our previous in vitro circular dichroism and fluorometric studies on the role of chaperone protein (acetylcholinesterase) in amyloid- peptide (A) aggregation1, and on A direct self assembly2, AFM and MALDI-ToF mass spectrometry approaches are here presented for the characterization of the dimension and molecular weight of A (1-42) aggregates. The results presented here provide nanometric resolution of the main structures characteristic of the several steps from monomeric A (1-42) to mature fibrils in vitro. Oligomeric globular aggregates of A (1-42) precede the appearance of protofibrils, the first fibrillar species. The most abundant form of A (1-42) fibril exhibits a nodular structure with a ~100-nm periodicity. These studies are in the frame of BISNES european project3, focused on the design, fabrication and operation of biomimetic nanostructured surfaces which precisely control the self-assembly of biomolecules in long-range architectures.

AMYLOID-b-PEPTIDE SELF ASSEMBLY KINETICS BY AFM AND MALDI-TOF MASS SPECTROMETRY

NALDI, MARINA;BARTOLINI, MANUELA;ANDRISANO, VINCENZA
2009

Abstract

Following our previous in vitro circular dichroism and fluorometric studies on the role of chaperone protein (acetylcholinesterase) in amyloid- peptide (A) aggregation1, and on A direct self assembly2, AFM and MALDI-ToF mass spectrometry approaches are here presented for the characterization of the dimension and molecular weight of A (1-42) aggregates. The results presented here provide nanometric resolution of the main structures characteristic of the several steps from monomeric A (1-42) to mature fibrils in vitro. Oligomeric globular aggregates of A (1-42) precede the appearance of protofibrils, the first fibrillar species. The most abundant form of A (1-42) fibril exhibits a nodular structure with a ~100-nm periodicity. These studies are in the frame of BISNES european project3, focused on the design, fabrication and operation of biomimetic nanostructured surfaces which precisely control the self-assembly of biomolecules in long-range architectures.
Atti del XXIII Congresso Nazionale della SCI
151
151
M.Naldi; M. Bartolini; D. Nicolau; V. Andrisano
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11585/83094
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