Self-assembly of ovalbumin into amyloid and non-amyloid fibrils.

Abstract:

:We study the fibrillation pathway of ovalbumin protein and report the simultaneous formation of several types of fibrils, with clear structural and physical differences. We compare the fibrillation mechanisms at low pH with and without salt, and follow the kinetics of fibrils growth by atomic force microscopy (AFM), static and dynamic light scattering (SLS, DLS), and small-angle X-ray scattering (SAXS). We show that, among the morphologies identified, long semiflexible amyloid fibrils (type I), with persistence length Lp∼3 μm, Young's modulus E∼2.8 GPa, and cross-β structure are formed. We also observe much more flexible fibrils (type III, Lp∼63 nm), that can assemble into multistranded ribbons with time. They show significantly lower intrinsic stiffness (1.1 GPa) and a secondary structure, which is not characteristic of the well-ordered amyloids, as determined by circular dichroism (CD), wide-angle X-ray scattering (WAXS), and attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR). In between these two main classes of fibrils, a third family, with intermediate flexibility (type II, Lp∼300 nm), is also resolved.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Lara C,Gourdin-Bertin S,Adamcik J,Bolisetty S,Mezzenga R

doi

10.1021/bm301481v

subject

Has Abstract

pub_date

2012-12-10 00:00:00

pages

4213-21

issue

12

eissn

1525-7797

issn

1526-4602

journal_volume

13

pub_type

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