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
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Lara C,Gourdin-Bertin S,Adamcik J,Bolisetty S,Mezzenga Rdoi
10.1021/bm301481vsubject
Has Abstractpub_date
2012-12-10 00:00:00pages
4213-21issue
12eissn
1525-7797issn
1526-4602journal_volume
13pub_type
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